Protein UniProt ENZYME entry Accepted name Alternative name(s) Reaction catalysed Cofactor(s) Comment(s) A0A0G2Q9F8 A0A0G2Q9F8 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. A0A0H2WWV6 A0A0H2WWV6 2.4.1.70 Poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase. Poly(ribitol-phosphate) N-acetylglucosaminyltransferase. UDP acetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase. n UDP-N-acetyl-alpha-D-glucosamine + 4-O-(D-ribitylphospho)(n)-di((2R)-1- glycerophospho)-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D- glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N- acetyl-alpha-D-glucosaminyl-D-ribitylphospho)(n)-di((2R)-1- glycerophospho)-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D- glucosaminyl-diphospho-ditrans,octacis-undecaprenol. -!- Involved in the biosynthesis of poly(ribitol phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. -!- This enzyme adds an N-acetyl-alpha-D-glucosamine to the hydroxyl group at the 2 position of the ribitol phosphate units. -!- Cf. EC 2.4.1.355. A0QNG1 A0QNG1 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. A0QPN2 A0QPN2 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. A0QSQ1 A0QSQ1 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. A0QWQ9 A0QWQ9 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. A0R082 A0R082 2.7.7.42 [Glutamine synthetase] adenylyltransferase. [Glutamate--ammonia-ligase] adenylyltransferase. Glutamate-ammonia-ligase adenylyltransferase. Glutamine-synthetase adenylyltransferase. ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine. -!- This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89). -!- The two activities are present on separate domains. A0R082 A0R082 2.7.7.89 [Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase. [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP. -!- This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42). -!- The two activities are present on separate domains. -!- Formerly EC 3.1.4.15. A0R0W9 A0R0W9 3.2.1.28 Alpha,alpha-trehalase. Trehalase. Alpha,alpha-trehalose + H(2)O = beta-D-glucose + alpha-D-glucose. -!- The enzyme is an anomer-inverting glucosidase that catalyzes the hydrolysis of the alpha-glucosidic O-linkage of alpha,alpha- trehalose, releasing initially equimolar amounts of alpha- and beta- D-glucose. -!- It is widely distributed in microorganisms, plants, invertebrates and vertebrates. A0R7H5 A0R7H5 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). A1JS01 A1JS01 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. A1KEU8 A1KEU8 2.7.1.175 Maltokinase. ATP + maltose = ADP + alpha-maltose 1-phosphate. Mg(2+). -!- Formerly EC 2.7.1.n8. A1KFE4 A1KFE4 3.5.4.30 dCTP deaminase (dUMP-forming). dCTP + 2 H(2)O = dUMP + diphosphate + NH(3). Mg(2+). -!- Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. -!- While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13 and EC 3.6.1.23), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. -!- This enzyme can also act as a dUTP diphosphatase, but more slowly. A1KFQ1 A1KFQ1 3.5.1.88 Peptide deformylase. PDF. Polypeptide deformylase. Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide. Fe(2+). -!- Requires at least a dipeptide for an efficient rate of reaction. -!- N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. -!- Differs in substrate specificity from EC 3.5.1.27 and EC 3.5.1.31. A1KFV6 A1KFV6 1.3.1.98 UDP-N-acetylmuramate dehydrogenase. UDP-GlcNAc-enoylpyruvate reductase. UDP-N-acetylenolpyruvoylglucosamine reductase. UDP-N-acetylglucosamine-enoylpyruvate reductase. Uridine diphospho-N-acetylglucosamine-enolpyruvate reductase. Uridine diphosphoacetylpyruvoylglucosamine reductase. UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-N-acetyl-3- O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH. FAD. -!- NADH can to a lesser extent replace NADPH. -!- Formerly EC 1.1.1.158. A1KG00 A1KG00 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. A1KG35 A1KG35 2.1.1.163 Demethylmenaquinone methyltransferase. 2-demethylmenaquinone methyltransferase. 2-heptaprenyl-1,4-naphthoquinone methyltransferase. Demethylmenaquinone C-methylase. A demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + S-adenosyl-L-homocysteine. -!- The enzyme catalyzes the last step in menaquinone biosynthesis. -!- It is able to accept substrates with varying polyprenyl side chain length (the chain length is determined by polyprenyl diphosphate synthase). -!- The enzyme from Escherichia coli also catalyzes the conversion of 2-methoxy-6-octaprenyl-1,4-benzoquinone to 5-methoxy-2-methyl-3- octaprenyl-1,4-benzoquinone during the biosynthesis of ubiquinone. -!- The enzyme probably acts on menaquinol rather than menaquinone. A1KGE8 A1KGE8 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. A1KGF0 A1KGF0 3.1.21.2 Deoxyribonuclease IV. Deoxyribonuclease IV (phage T4-induced). Endodeoxyribonuclease IV (phage T(4)-induced). Endodeoxyribonuclease IV (phage T4-induced). Endonuclease II. Endonuclease IV. Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. -!- The enzyme is an apurinic/apyrimidinic (AP) site endonuclease that primes DNA repair synthesis at AP sites. -!- It specifically cleaves the DNA backbone at AP sites and also removes 3' DNA-blocking groups such as 3' phosphates, 3' phosphoglycolates, and 3' alpha,beta-unsaturated aldehydes that arise from oxidative base damage and the activity of combined glycosylase/lyase enzymes. -!- It is also the only known repair enzyme that is able to cleave the DNA backbone 5' of the oxidative lesion alpha-deoxyadenosine. -!- The enzyme has a strong preference for single-stranded DNA. -!- Formerly EC 3.1.4.30. A1KGL4 A1KGL4 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. A1KH91 A1KH91 2.1.2.3 Phosphoribosylaminoimidazolecarboxamide formyltransferase. 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4- imidazolecarboxamide formyltransferase. 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase. 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase. 5-amino-4-imidazolecarboxamide ribonucleotide transformylase. 5-amino-4-imidazolecarboxamide ribotide transformylase. AICAR formyltransferase. AICAR transformylase. Aminoimidazolecarboxamide ribonucleotide transformylase. 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide. A1KH91 A1KH91 3.5.4.10 IMP cyclohydrolase. IMP synthetase. Inosinicase. IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. A1KHE8 A1KHE8 2.1.1.182 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase. 4 S-adenosyl-L-methionine + adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(1518)/N(6)- dimethyladenine(1519) in 16S rRNA. -!- KsgA introduces the most highly conserved ribosomal RNA modification, the dimethylation of adenine(1518) and adenine(1519) in 16S rRNA. -!- Strains lacking the methylase are resistant to kasugamycin. -!- Formerly EC 2.1.1.48. A1KHE9 A1KHE9 2.7.1.148 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase. CDP-ME kinase. CMK. ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Mn(2+) or Mg(2+). -!- Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. A1KHN9 A1KHN9 3.1.3.11 Fructose-bisphosphatase. Fructose 1,6-bisphosphatase. Hexose diphosphatase. D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. -!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. A1KHS4 A1KHS4 2.1.1.14 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. Cobalamin-independent methionine synthase. Homocysteine methylase. Methionine synthase (cobalamin-independent). Methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase. Tetrahydropteroylglutamate-homocysteine transmethylase. 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. Zn(2+). -!- Requires phosphate. -!- The enzyme from Escherichia coli also requires a reducing system. -!- Unlike EC 2.1.1.13 this enzyme does not contain cobalamin. A1KIM7 A1KIM7 5.3.1.1 Triose-phosphate isomerase. Phosphotriose isomerase. Triose phosphoisomerase. Triosephosphate isomerase. Triosephosphate mutase. D-glyceraldehyde 3-phosphate = glycerone phosphate. A1KIN7 A1KIN7 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. A1KJ01 A1KJ01 6.3.3.3 Dethiobiotin synthase. DTB synthetase. ATP + 7,8-diaminononanoate + CO(2) = ADP + phosphate + dethiobiotin. -!- CTP has half the activity of ATP. A1KJ27 A1KJ27 4.1.1.48 Indole-3-glycerol-phosphate synthase. Indoleglycerol phosphate synthetase. 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C- (3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. -!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.3.27, EC 4.2.1.20 and EC 5.3.1.24). A1KJP9 A1KJP9 2.3.3.9 Malate synthase. Glyoxylate transacetase. Glyoxylate transacetylase. Glyoxylic transacetase. L-malate glyoxylate-lyase (CoA-acetylating). Malate condensing enzyme. Malate synthetase. Malic synthetase. Malic-condensing enzyme. Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA. -!- The enzyme catalyzes the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. -!- Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO(2). -!- Formerly EC 4.1.3.2. A1KJR2 A1KJR2 3.5.1.5 Urease. Urea + H(2)O = CO(2) + 2 NH(3). Ni(2+). A1KJX3 A1KJX3 1.11.1.21 Catalase peroxidase. (1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O. -!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. A1KKH3 A1KKH3 6.3.1.13 L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase. MshC ligase. Mycothiol ligase. 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-(2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl)-1D-myo- inositol + AMP + diphosphate. -!- This enzyme is a key enzyme in the biosynthesis of mycothiol, a small molecular weight thiol found in Mycobacteria spp. and other actinomycetes. -!- Mycothiol plays a fundamental role in these organisms by helping to provide protection from the effects of reactive oxygen species and electrophiles, including many antibiotics. -!- The enzyme may represent a novel target for new classes of antituberculars. -!- Formerly EC 6.1.1.n1. A1KKJ6 A1KKJ6 2.4.1.227 Undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase. MurG transferase. UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl- undecaprenol N-acetylglucosamine transferase. Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase. UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D- Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma- D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. -!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. A1KKJ8 A1KKJ8 6.3.2.9 UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase. D-glutamate ligase. D-glutamate-adding enzyme. MurD synthetase. UDP-Mur-NAC-L-Ala:D-Glu ligase. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase. UDP-N-acetylmuramoylalanine--D-glutamate ligase. Uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase. ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate. -!- Involved in the synthesis of a cell-wall peptide in bacteria. A1KKK8 A1KKK8 2.1.1.199 16S rRNA (cytosine(1402)-N(4))-methyltransferase. S-adenosyl-L-methionine + cytosine(1402) in 16S rRNA = S-adenosyl-L- homocysteine + N(4)-methylcytosine(1402) in 16S rRNA. -!- RsmH catalyzes the N(4)-methylation of cytosine(1402) and RsmI (EC 2.1.1.198) catalyzes the 2'-O-methylation of cytosine(1402) in 16S rRNA. -!- Both methylations are necessary for efficient translation initiation at the UUG and GUG codons. A1KKQ5 A1KKQ5 3.4.11.1 Leucyl aminopeptidase. Cytosol aminopeptidase. Leucine aminopeptidase. Peptidase S. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Zn(2+). -!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC 3.4.1.1. A1KKQ5 A1KKQ5 3.4.11.10 Bacterial leucyl aminopeptidase. Aeromonas proteolytica aminopeptidase. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Zn(2+). -!- Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus. -!- Belongs to peptidase families M17 and M28. A1KLE1 A1KLE1 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. A1KLF8 A1KLF8 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. A1KLQ3 A1KLQ3 6.1.1.7 Alanine--tRNA ligase. Alanine translase. Alanyl-tRNA synthetase. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). A1KLT2 A1KLT2 2.4.2.7 Adenine phosphoribosyltransferase. AMP diphosphorylase. AMP pyrophosphorylase. APRT. Transphosphoribosidase. AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. -!- 5-amino-4-imidazolecarboxamide can replace adenine. A1KLV6 A1KLV6 4.3.3.6 Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing). D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate. -!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants. A1KMC6 A1KMC6 2.7.7.8 Polyribonucleotide nucleotidyltransferase. Polynucleotide phosphorylase. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. -!- ADP, IDP, GDP, UDP and CDP can act as donors. A1KML3 A1KML3 1.17.7.3 (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin). (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase. (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H(2)O + oxidized flavodoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin. -!- Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria. -!- Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1). A1KML5 A1KML5 1.1.1.267 1-deoxy-D-xylulose-5-phosphate reductoisomerase. 1-deoxyxylulose-5-phosphate reductoisomerase. DXP-reductoisomerase. 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + NADPH. Mg(2+) or cobalt cation or Mn(2+). -!- The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. -!- The mechanism has been shown to be a retroaldol/aldol reaction. A1KMM4 A1KMM4 2.1.1.192 23S rRNA (adenine(2503)-C(2))-methyltransferase. (1) 2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe- 2S] ferredoxin. (2) 2 S-adenosyl-L-methionine + adenine(37) in tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 oxidized [2Fe-2S] ferredoxin. Iron-sulfur. -!- This enzyme is a member of the 'AdoMet radical' (radical SAM) family. -!- S-adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group. -!- RlmN first transfers an CH(2) group to a conserved cysteine (Cys(355) in Escherichia coli), the generated radical from a second S-adenosyl- L-methionine then attacks the methyl group, exctracting a hydrogen. -!- The formed radical forms a covalent intermediate with the adenine group of the tRNA. -!- RlmN is an endogenous enzyme used by the cell to refine functions of the ribosome in protein synthesis. -!- The enzyme methylates adenosine by a radical mechanism with CH(2) from the S-adenosyl-L-methionine and retention of the hydrogen at C-2 of adenosine(2503) of 23S rRNA. -!- It will also methylate 8-methyladenosine(2503) of 23S rRNA (cf. EC 2.1.1.224). A1KNQ0 A1KNQ0 3.3.1.1 Adenosylhomocysteinase. Adenosylhomocysteine hydrolase. AdoHcyase. S-adenosylhomocysteinase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine synthase. SAHase. S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine. NAD(+). -!- The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4. A1KP49 A1KP49 1.5.1.5 Methylenetetrahydrofolate dehydrogenase (NADP(+)). 5,10-methylenetetrahydrofolate + NADP(+) = 5,10- methenyltetrahydrofolate + NADPH. A1KP49 A1KP49 3.5.4.9 Methenyltetrahydrofolate cyclohydrolase. 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate. A1KP65 A1KP65 3.1.3.12 Trehalose-phosphatase. Trehalose 6-phosphate phosphatase. Trehalose 6-phosphate + H(2)O = trehalose + phosphate. A1KPC8 A1KPC8 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. A1KPR8 A1KPR8 2.7.7.60 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase. MCT. MEP cytidylyltransferase. CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Mn(2+) or Mg(2+). -!- ATP or UTP can replace CTP, but both are less effective. -!- GTP and TTP are not substrates. -!- Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. A1KPS2 A1KPS2 2.7.7.85 Diadenylate cyclase. Cyclic-di-AMP synthase. 2 ATP = 2 diphosphate + cyclic di-3',5'-adenylate. -!- Cyclic di-3',5'-adenylate is a bioactive molecule produced by some bacteria and archaea, which may function as a secondary signaling molecule. -!- The intracellular bacterial pathogen Listeria monocytogenes secretes it into the host's cytosol, where it triggers a cytosolic pathway of innate immunity. A1KQH3 A1KQH3 4.2.1.51 Prephenate dehydratase. Prephenate = phenylpyruvate + H(2)O + CO(2). -!- This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate. A3M1G4 A3M1G4 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. A4F7G2 A4F7G2 1.4.3.5 Pyridoxal 5'-phosphate synthase. PMP oxidase. Pyridoxamine 5'-phosphate oxidase. Pyridoxamine phosphate oxidase. Pyridoxamine-phosphate oxidase. Pyridoxine (pyridoxamine) 5'-phosphate oxidase. Pyridoxine (pyridoxamine)phosphate oxidase. (1) Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2). (2) Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-phosphate + H(2)O(2). FMN. -!- In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5. A4FBD3 A4FBD3 6.1.1.7 Alanine--tRNA ligase. Alanine translase. Alanyl-tRNA synthetase. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). A4FBY4 A4FBY4 6.3.1.19 Prokaryotic ubiquitin-like protein ligase. Proteasome accessory factor A. Pup ligase. Pup--protein ligase. Pup-conjugating enzyme. ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L- lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-like protein]- gamma-L-glutamyl)-[protein]-L-lysine. -!- The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum. -!- It catalyzes the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an epsilon-amino group of a lysine residue of the target protein and the gamma- carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup). -!- The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation. -!- Formerly EC 6.3.2.n2. A4FIR1 A4FIR1 1.11.1.21 Catalase peroxidase. (1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O. -!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. A4FMQ5 A4FMQ5 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. A4FN29 A4FN29 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. A4FPJ2 A4FPJ2 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. A4FQV7 A4FQV7 4.1.1.32 Phosphoenolpyruvate carboxykinase (GTP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2). -!- ITP can act as phosphate donor. A4FR54 A4FR54 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). A5F5X0 A5F5X0 7.2.1.1 NADH:ubiquinone reductase (Na(+)-transporting). Na(+)-NQR. Na(+)-translocating NADH-quinone reductase. NADH + ubiquinone + n Na(+)(In) = NAD(+) + ubiquinol + n Na(+)(Out). FAD; FMN; Iron-sulfur; Riboflavin. -!- An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster. -!- Formerly EC 1.6.5.8. A5F5Y7 A5F5Y7 7.2.1.1 NADH:ubiquinone reductase (Na(+)-transporting). Na(+)-NQR. Na(+)-translocating NADH-quinone reductase. NADH + ubiquinone + n Na(+)(In) = NAD(+) + ubiquinol + n Na(+)(Out). FAD; FMN; Iron-sulfur; Riboflavin. -!- An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster. -!- Formerly EC 1.6.5.8. A5TY85 A5TY85 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. A6QF82 A6QF82 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. A6QFE3 A6QFE3 6.2.1.54 D-alanine--[D-alanyl-carrier protein] ligase. ATP + D-alanine + holo-[D-alaninyl-carrier protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier protein]. -!- The enzyme is involved in the modification of wall teichoic acids, as well as type I and IV lipoteichoic acids, with D-alanine residues. -!- It activates D-alanine using ATP to form a high-energy (D-alanyl)adenylate intermediate and subsequently transfers the alanyl moiety to the phosphopantheinyl prosthetic group of a D-alanyl-carrier protein (DltC). A6QFH3 A6QFH3 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. A6QGC0 A6QGC0 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. A6QHK1 A6QHK1 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. A6QHX1 A6QHX1 4.1.1.49 Phosphoenolpyruvate carboxykinase (ATP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2). A6QIV7 A6QIV7 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. A6QJK4 A6QJK4 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. A6QK93 A6QK93 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. A6TDR7 A6TDR7 2.1.2.10 Aminomethyltransferase. Glycine synthase. Glycine-cleavage system T-protein. Tetrahydrofolate aminomethyltransferase. [Protein]-S(8)-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH(3). -!- A component, with EC 1.4.4.2 and EC 1.8.1.4, of the glycine cleavage system, formerly known as glycine synthase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. A7FKP6 A7FKP6 5.4.2.11 Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). 2,3-diphosphoglycerate dependent phosphoglycerate mutase. Cofactor dependent phosphoglycerate mutase. PGAM. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. -!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. A7HD43 A7HD43 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. A7MRY4 A7MRY4 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. A7N6S2 A7N6S2 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. A7X5Y6 A7X5Y6 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. A7Z0L6 A7Z0L6 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). A7Z7J8 A7Z7J8 1.1.1.37 Malate dehydrogenase. Malic dehydrogenase. (S)-malate + NAD(+) = oxaloacetate + NADH. -!- Also oxidizes some other 2-hydroxydicarboxylic acids. A7Z8Y1 A7Z8Y1 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. A7ZPV7 A7ZPV7 6.1.1.21 Histidine--tRNA ligase. Histidine translase. Histidyl-tRNA synthetase. ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). A7ZR34 A7ZR34 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. A7ZRX6 A7ZRX6 5.3.1.12 Glucuronate isomerase. D-glucuronate isomerase. Uronate isomerase. Uronic acid isomerase. Uronic isomerase. D-glucuronate = D-fructuronate. -!- Also converts D-galacturonate to D-tagaturonate. A8ACN8 A8ACN8 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. A8AD67 A8AD67 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. A8AG06 A8AG06 2.5.1.55 3-deoxy-8-phosphooctulonate synthase. 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating). 2-dehydro-3-deoxy-phosphooctonate aldolase. 2-keto-3-deoxy-8-phosphooctonic synthetase. 3-deoxy-D-manno-octulosonate-8-phosphate synthase. 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase. 3-deoxy-D-mannooctulosonate-8-phosphate synthetase. 3-deoxyoctulosonic 8-phosphate synthetase. KDO-8-P synthase. KDO-8-phosphate synthetase. KDOP synthase. Phospho-2-keto-3-deoxyoctonate aldolase. Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 3-deoxy-D-manno- octulosonate 8-phosphate + phosphate. -!- Formerly EC 4.1.2.16. A8AQ65 A8AQ65 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. A8G8E8 A8G8E8 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. B0R4C8 B0R4C8 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. B0R502 B0R502 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. B0R6B9 B0R6B9 4.2.1.96 4a-hydroxytetrahydrobiopterin dehydratase. 4-alpha-hydroxy-tetrahydropterin dehydratase. Pterin-4-alpha-carbinolamine dehydratase. Tetrahydrobiopterin dehydratase. (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro- 4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro- 6H-pterin + H(2)O. -!- Catalyzes the dehydration of 4a-hydroxytetrahydrobiopterins. B0R7F9 B0R7F9 4.1.1.31 Phosphoenolpyruvate carboxylase. PEP carboxylase. PEPCase. Phosphoenolpyruvic carboxylase. Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-). -!- This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. -!- The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate. B0RVK5 B0RVK5 5.4.2.2 Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent). Glucose phosphomutase. Phosphoglucose mutase. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. -!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1. B0RVK5 B0RVK5 5.4.2.8 Phosphomannomutase. Phosphomannose mutase. Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. -!- Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.7. B0VLX4 B0VLX4 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase. Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase. (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. -!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211). B0VLX4 B0VLX4 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). B0VLX4 B0VLX4 5.1.2.3 3-hydroxybutyryl-CoA epimerase. (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. B0VLX4 B0VLX4 5.3.3.8 Delta(3)-Delta(2)-enoyl-CoA isomerase. 3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase. (1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. -!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters. B0VLZ5 B0VLZ5 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. B0VMY0 B0VMY0 2.1.1.170 16S rRNA (guanine(527)-N(7))-methyltransferase. S-adenosyl-L-methionine + guanine(527) in 16S rRNA = S-adenosyl-L- homocysteine + N(7)-methylguanine(527) in 16S rRNA. -!- The enzyme specifically methylates guanine(527) at N(7) in 16S rRNA. B0VN00 B0VN00 2.7.4.25 (d)CMP kinase. dCMP kinase. Deoxycytidine monophosphokinase. Deoxycytidylate kinase. ATP + (d)CMP = ADP + (d)CDP. -!- The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. -!- Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22. -!- The enzyme phosphorylates dCMP nearly as well as it does CMP. B0VNK4 B0VNK4 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. B0VPG4 B0VPG4 2.7.8.13 Phospho-N-acetylmuramoyl-pentapeptide-transferase. MraY transferase. Phospho-MurNAc-pentapeptide transferase. Phospho-N-acetylmuramoyl pentapeptide translocase. Phospho-NAc-muramoyl-pentapeptide translocase (UMP). Phosphoacetylmuramoylpentapeptide translocase. Phosphoacetylmuramoylpentapeptidetransferase. UDP-MurNAc-Ala-gamma-DGlu-Lys-DAla-DAla:undecaprenylphosphate transferase. UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C(55)-isoprenoid alcohol transferase. UDP-MurNAc-pentapeptide phosphotransferase. UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- diphosphoundecaprenol. -!- In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-center. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. B0VPN2 B0VPN2 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. B0VQ53 B0VQ53 1.17.7.4 4-hydroxy-3-methylbut-2-enyl diphosphate reductase. (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase. HMBPP reductase. (1) Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). (2) Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). Iron-sulfur. -!- Forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. -!- This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. -!- This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. -!- The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate. -!- Formerly EC 1.17.1.2. B0VQI4 B0VQI4 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. B0VQI5 B0VQI5 2.5.1.55 3-deoxy-8-phosphooctulonate synthase. 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating). 2-dehydro-3-deoxy-phosphooctonate aldolase. 2-keto-3-deoxy-8-phosphooctonic synthetase. 3-deoxy-D-manno-octulosonate-8-phosphate synthase. 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase. 3-deoxy-D-mannooctulosonate-8-phosphate synthetase. 3-deoxyoctulosonic 8-phosphate synthetase. KDO-8-P synthase. KDO-8-phosphate synthetase. KDOP synthase. Phospho-2-keto-3-deoxyoctonate aldolase. Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 3-deoxy-D-manno- octulosonate 8-phosphate + phosphate. -!- Formerly EC 4.1.2.16. B0VQI6 B0VQI6 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. B0VRK7 B0VRK7 1.3.1.98 UDP-N-acetylmuramate dehydrogenase. UDP-GlcNAc-enoylpyruvate reductase. UDP-N-acetylenolpyruvoylglucosamine reductase. UDP-N-acetylglucosamine-enoylpyruvate reductase. Uridine diphospho-N-acetylglucosamine-enolpyruvate reductase. Uridine diphosphoacetylpyruvoylglucosamine reductase. UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-N-acetyl-3- O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH. FAD. -!- NADH can to a lesser extent replace NADPH. -!- Formerly EC 1.1.1.158. B0VS13 B0VS13 6.3.5.7 Glutaminyl-tRNA synthase (glutamine-hydrolyzing). GatCAB. GatDE. GatFAB. Glu-AdT. Glu-tRNA(Gln) amidotransferase. Glutamyl-tRNA(Gln) amidotransferase. ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. -!- In systems lacking discernible glutamine--tRNA ligase (EC 6.1.1.18), glutaminyl-tRNA(Gln) is formed by a two-enzyme system. -!- In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln). -!- The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl- tRNA(Glu) is not a substrate for this enzyme). -!- A glutaminase subunit (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. -!- Some bacterial GatCAB complexes also has the activity of EC 6.3.5.6. B0VT30 B0VT30 5.1.1.7 Diaminopimelate epimerase. LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. B0VT70 B0VT70 6.3.3.1 Phosphoribosylformylglycinamidine cyclo-ligase. AIR synthase. AIR synthetase. AIRS. Phosphoribosyl-aminoimidazole synthetase. Phosphoribosylaminoimidazole synthetase. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. B0VT89 B0VT89 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). B0VTE3 B0VTE3 2.7.2.8 Acetylglutamate kinase. ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. B0VU92 B0VU92 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. B0VUQ9 B0VUQ9 4.1.1.37 Uroporphyrinogen decarboxylase. Uroporphyrinogen III decarboxylase. Uroporphyrinogen-III carboxy-lyase. Uroporphyrinogen III = coproporphyrinogen + 4 CO(2). -!- Acts on a number of porphyrinogens. B1XHW1 B1XHW1 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. B1XL18 B1XL18 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. B1XLK6 B1XLK6 1.2.1.70 Glutamyl-tRNA reductase. L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. -!- Forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway, which is used in most eubacteria, and in all archaebacteria, algae and plants. -!- However, in the alpha-proteobacteria EC 2.3.1.37 is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. -!- This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. -!- Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. B1XN08 B1XN08 1.8.4.8 Phosphoadenylyl-sulfate reductase (thioredoxin). 3'-phosphoadenylylsulfate reductase. PAdoPS reductase. PAPS reductase. PAPS reductase, thioredoxin-dependent. PAPS sulfotransferase. Phosphoadenosine-phosphosulfate reductase. Thioredoxin:3'-phospho-adenylylsulfate reductase. Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase. Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. -!- Specific for PAPS. -!- The enzyme from Escherichia coli will use thioredoxins from other species. -!- Formerly EC 1.8.99.4. B1XN71 B1XN71 4.2.1.96 4a-hydroxytetrahydrobiopterin dehydratase. 4-alpha-hydroxy-tetrahydropterin dehydratase. Pterin-4-alpha-carbinolamine dehydratase. Tetrahydrobiopterin dehydratase. (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro- 4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro- 6H-pterin + H(2)O. -!- Catalyzes the dehydration of 4a-hydroxytetrahydrobiopterins. B1XP53 B1XP53 6.1.1.15 Proline--tRNA ligase. Proline translase. Prolyl-tRNA synthetase. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). B1XP90 B1XP90 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). B1XPE2 B1XPE2 3.1.3.5 5'-nucleotidase. A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate. -!- Wide specificity for 5'-nucleotides. B1XPG7 B1XPG7 1.17.7.4 4-hydroxy-3-methylbut-2-enyl diphosphate reductase. (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase. HMBPP reductase. (1) Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). (2) Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). Iron-sulfur. -!- Forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. -!- This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. -!- This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. -!- The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate. -!- Formerly EC 1.17.1.2. B1XPX8 B1XPX8 6.1.1.19 Arginine--tRNA ligase. Arginine translase. Arginyl-tRNA synthetase. ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). B5XZ79 B5XZ79 4.3.1.3 Histidine ammonia-lyase. Histidase. Histidinase. Histidine alpha-deaminase. L-histidine = urocanate + NH(3). -!- Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.23, EC 4.3.1.24 and EC 4.3.1.25. -!- Catalyzes the first step in the degradation of histidine and the product, urocanic acid, is further metabolized to glutamate. B5Y275 B5Y275 5.4.2.7 Phosphopentomutase. Deoxyribomutase. Deoxyribose phosphomutase. Phosphodeoxyribomutase. Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. -!- Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D- ribose 5-phosphate. -!- Alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5- bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.6. B7MDM9 B7MDM9 4.1.1.49 Phosphoenolpyruvate carboxykinase (ATP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2). B7UR12 B7UR12 2.4.2.1 Purine-nucleoside phosphorylase. Inosine phosphorylase. PNPase. (1) Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. (2) Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate. -!- Specificity not completely determined. -!- Can also catalyze ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5. B8GZM2 B8GZM2 2.7.7.65 Diguanylate cyclase. DGC. 2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate. Mg(2+); Mn(2+). -!- Can be activated by BeF3, a phosphoryl mimic, which results in dimerization. -!- Dimerization is required but is not sufficient for diguanylate- cyclase activity. -!- Cyclic di-3',5'-guanylate is an intracellular signaling molecule that controls motility and adhesion in bacterial cells; it was first identified as having a positive allosteric effect on EC 2.4.1.12. C0SP93 C0SP93 2.1.3.15 Acetyl-CoA carboxytransferase. [Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl- CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl- CoA. -!- The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. -!- In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2). -!- Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3). C1KYU1 C1KYU1 4.2.1.59 3-hydroxyacyl-[acyl-carrier-protein] dehydratase. (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase. Beta-hydroxyoctanoyl thioester dehydratase. Beta-hydroxyoctanoyl-ACP-dehydrase. Beta-hydroxyoctanoyl-acyl carrier protein dehydrase. D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase. A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O. -!- This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- The enzyme uses fatty acyl thioesters of ACP in vivo. -!- Different forms of the enzyme may have preferences for substrates with different chain length. -!- For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. -!- Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14. -!- Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0). -!- FabZ, but not FabA, can also accept unsaturated substrates. -!- Formerly EC 4.2.1.58, EC 4.2.1.60 and EC 4.2.1.61. D0ZV89 D0ZV89 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. D4GYZ1 D4GYZ1 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. I6WZK7 I6WZK7 1.16.3.1 Ferroxidase. Ceruloplasmin. HEPH. Hephaestin. 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. Cu cation. I6Y4D2 I6Y4D2 3.5.1.28 N-acetylmuramoyl-L-alanine amidase. Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. -!- Formerly EC 3.4.12.5, EC 3.4.17.7 and EC 3.4.19.10. I6Y9Q3 I6Y9Q3 2.3.3.5 2-methylcitrate synthase. 2-methylcitrate oxaloacetate-lyase. MCS. Methylcitrate synthase. Methylcitrate synthetase. Propanoyl-CoA + H(2)O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3- tricarboxylate + CoA. -!- The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. -!- The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme is distinct from EC 2.3.3.1. -!- Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate. -!- Formerly EC 4.1.3.31. I6Y9Q3 I6Y9Q3 2.3.3.16 Citrate synthase (unknown stereospecificity). Citrate condensing enzyme. Citrate synthetase. Citric synthase. Citric-condensing enzyme. Citrogenase. CoA-acetylating citrate oxaloacetate-lyase. Condensing enzyme. Oxalacetic transacetase. Oxaloacetate transacetase. Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. -!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3). L7N653 L7N653 3.5.1.28 N-acetylmuramoyl-L-alanine amidase. Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. -!- Formerly EC 3.4.12.5, EC 3.4.17.7 and EC 3.4.19.10. O05268 O05268 1.18.1.2 Ferredoxin--NADP(+) reductase. 2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH. FAD. -!- In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin. -!- Formerly EC 1.6.7.1 and EC 1.6.99.4. O05442 O05442 3.2.2.5 NAD(+) glycohydrolase. ADP-ribosyl cyclase. Beta-NAD(+) glycohydrolase. Diphosphopyridine nucleosidase. DPN hydrolase. DPNase. NAD glycohydrolase. NAD nucleosidase. NAD(+) nucleosidase. NADase. Nicotinamide adenine dinucleotide glycohydrolase. Nicotinamide adenine dinucleotide nucleosidase. NAD(+) + H(2)O = ADP-D-ribose + nicotinamide. -!- This enzyme catalyzes the hydrolysis of NAD(+), without associated ADP-ribosyl cyclase activity (unlike the metazoan enzyme EC 3.2.2.6, bifunctional ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase). -!- The enzyme from Group A streptococci has been implicated in the pathogenesis of diseases such as streptococcal toxic shock-like syndrome (STSS) and necrotizing fasciitis. -!- The enzyme from the venom of the snake Agkistrodon acutus also catalyzes EC 3.6.1.5. O05518 O05518 2.3.1.234 N(6)-L-threonylcarbamoyladenine synthase. T6A synthase. L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N(6)-L- threonylcarbamoyladenine(37) in tRNA. -!- The enzyme is involved in the synthesis of N(6)- threonylcarbamoyladenosine(37) in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNA(Ile), tRNA(Thr), tRNA(Asn), tRNA(Lys), tRNA(Ser) and tRNA(Arg). -!- Formerly EC 2.6.99.4. O05520 O05520 4.6.1.17 Cyclic pyranopterin monophosphate synthase. (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate. -!- The enzyme catalyzes an early step in the biosynthesis of the molybdenum cofactor (MoCo). -!- Formerly EC 4.1.99.18. O05982 O05982 2.7.4.25 (d)CMP kinase. dCMP kinase. Deoxycytidine monophosphokinase. Deoxycytidylate kinase. ATP + (d)CMP = ADP + (d)CDP. -!- The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. -!- Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22. -!- The enzyme phosphorylates dCMP nearly as well as it does CMP. O06159 O06159 2.3.1.168 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase. Dihydrolipoyl transacylase. 2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine. -!- A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalyzed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. -!- In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine. O06457 O06457 6.3.4.18 5-(carboxyamino)imidazole ribonucleotide synthase. N(5)-CAIR synthetase. N(5)-carboxyaminoimidazole ribonucleotide synthetase. ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole. -!- In Escherichia coli, this enzyme, along with EC 5.4.99.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates. -!- Carboxyphosphate is the putative acyl phosphate intermediate. -!- Involved in the late stages of purine biosynthesis. O06491 O06491 6.3.5.7 Glutaminyl-tRNA synthase (glutamine-hydrolyzing). GatCAB. GatDE. GatFAB. Glu-AdT. Glu-tRNA(Gln) amidotransferase. Glutamyl-tRNA(Gln) amidotransferase. ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. -!- In systems lacking discernible glutamine--tRNA ligase (EC 6.1.1.18), glutaminyl-tRNA(Gln) is formed by a two-enzyme system. -!- In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln). -!- The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl- tRNA(Glu) is not a substrate for this enzyme). -!- A glutaminase subunit (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. -!- Some bacterial GatCAB complexes also has the activity of EC 6.3.5.6. O07012 O07012 3.2.1.23 Beta-galactosidase. Exo-(1->4)-beta-D-galactanase. Lactase. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D- galactosides. -!- Some enzymes in this group hydrolyze alpha-L-arabinosides; some animal enzymes also hydrolyze beta-D-fucosides and beta-D-glucosides (cf. EC 3.2.1.108). O07584 O07584 2.3.1.n4 1-acyl-sn-glycerol-3-phosphate acyltransferase. Acyl-[acyl-carrier-protein] + 1-acyl-sn-glycerol 3-phosphate = [acyl- carrier-protein] + 1,2-diacyl-sn-glycerol 3-phosphate. O07717 O07717 4.1.3.1 Isocitrate lyase. ICL. Isocitrase. Isocitratase. Isocitrate glyoxylate-lyase. Isocitritase. Isocitrate = succinate + glyoxylate. -!- The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3- tricarboxylate. O08309 O08309 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). O08314 O08314 2.4.2.29 tRNA-guanine(34) transglycosylase. Guanine insertion enzyme. Q-insertase. Queuine tRNA-ribosyltransferase. Queuine(34) transfer ribonucleate ribosyltransferase. TGT. tRNA guanine(34) transglycosidase. tRNA transglycosylase. (1) Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. (2) Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine(34) in tRNA + guanine. -!- Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. -!- In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. -!- In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ(1), which is ultimately modified to queuine. -!- The eubacterial enzyme can also use an earlier intermediate, preQ(0), to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn). -!- This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway. O08357 O08357 3.5.2.3 Dihydroorotase. Carbamoylaspartic dehydrase. DHOase. (S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate. O08359 O08359 2.4.2.10 Orotate phosphoribosyltransferase. OPRT. Orotidine-5'-phosphate diphosphorylase. Orotidine-5'-phosphate pyrophosphorylase. Orotidylic acid phosphorylase. Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. -!- The enzyme from higher eukaryotes also catalyzes the reaction listed as EC 4.1.1.23. O08394 O08394 1.6.2.4 NADPH--hemoprotein reductase. Aldehyde reductase (NADPH-dependent). CPR. Cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent). Cytochrome P450 reductase. Dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase. FAD-cytochrome c reductase. Ferrihemoprotein P-450 reductase. NADP--cytochrome c reductase. NADP--cytochrome reductase. NADPH--cytochrome c oxidoreductase. NADPH--cytochrome c reductase. NADPH--cytochrome P450 oxidoreductase. NADPH--cytochrome P450 reductase. NADPH--ferricytochrome c oxidoreductase. NADPH--ferrihemoprotein reductase. NADPH-dependent cytochrome c reductase. NADPH:ferrihemoprotein oxidoreductase. NADPH:P450 reductase. Reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase. Reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate). TPNH(2) cytochrome c reductase. TPNH-cytochrome c reductase. NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein. FAD; FMN. -!- This enzyme catalyzes the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P450 monooxygenases (e.g. EC 1.14.14.1) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. -!- It also reduces cytochrome b5 and cytochrome c. -!- The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. O08394 O08394 1.14.14.1 Unspecific monooxygenase. Aryl hydrocarbon hydroxylase. Aryl-4-monooxygenase. Cytochrome P450. Flavoprotein-linked monooxygenase. Microsomal monooxygenase. Microsomal P450. Xenobiotic monooxygenase. RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O. Heme-thiolate. -!- Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. -!- Together with EC 1.6.2.4, it forms a system in which two reducing equivalents are supplied by NADPH. -!- Some of the reactions attributed to EC 1.14.15.3 belong here. -!- Formerly EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8 and EC 1.99.1.1. O25008 O25008 2.8.1.7 Cysteine desulfurase. Cysteine desulfurylase. L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. Pyridoxal 5'-phosphate. -!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. O25029 O25029 3.6.4.13 RNA helicase. ATP + H(2)O = ADP + phosphate. -!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase). O25121 O25121 2.2.1.7 1-deoxy-D-xylulose-5-phosphate synthase. 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating). 1-deoxyxylulose-5-phosphate synthase. DXP-synthase. Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO(2). Thiamine diphosphate. -!- The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. -!- Formerly EC 4.1.3.37. O25130 O25130 2.6.1.92 UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase. UDP-4-dehydro-6-deoxy-D-glucose transaminase. UDP-beta-L-threo-pentapyranos-4-ulose transaminase. UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate. Pyridoxal 5'-phosphate. -!- The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. -!- The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose, UDP-beta- L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose. -!- Cf. EC 2.6.1.34, which catalyzes a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP. O25235 O25235 2.7.8.13 Phospho-N-acetylmuramoyl-pentapeptide-transferase. MraY transferase. Phospho-MurNAc-pentapeptide transferase. Phospho-N-acetylmuramoyl pentapeptide translocase. Phospho-NAc-muramoyl-pentapeptide translocase (UMP). Phosphoacetylmuramoylpentapeptide translocase. Phosphoacetylmuramoylpentapeptidetransferase. UDP-MurNAc-Ala-gamma-DGlu-Lys-DAla-DAla:undecaprenylphosphate transferase. UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C(55)-isoprenoid alcohol transferase. UDP-MurNAc-pentapeptide phosphotransferase. UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- diphosphoundecaprenol. -!- In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-center. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. O25595 O25595 5.1.1.1 Alanine racemase. L-alanine = D-alanine. Pyridoxal 5'-phosphate. O25664 O25664 2.7.7.60 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase. MCT. MEP cytidylyltransferase. CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Mn(2+) or Mg(2+). -!- ATP or UTP can replace CTP, but both are less effective. -!- GTP and TTP are not substrates. -!- Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. O25664 O25664 4.6.1.12 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. MECDP-synthase. 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl- D-erythritol 2,4-cyclodiphosphate + CMP. Mn(2+) or Mg(2+). -!- Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. O25806 O25806 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. O26103 O26103 1.1.1.262 4-hydroxythreonine-4-phosphate dehydrogenase. 4-(phosphohydroxy)-L-threonine dehydrogenase. L-threonine 4-phosphate dehydrogenase. NAD(+)-dependent threonine 4-phosphate dehydrogenase. 4-phosphooxy-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO(2) + NADH. -!- The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria. O28471 O28471 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. O30245 O30245 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. O31149 O31149 2.7.3.9 Phosphoenolpyruvate--protein phosphotransferase. Enzyme I of the phosphotransferase system. Phosphoenolpyruvate sugar phosphotransferase enzyme I. Phosphoenolpyruvate--protein phosphatase. Phosphopyruvate--protein factor phosphotransferase. Phosphopyruvate--protein phosphotransferase. Sugar--PEP phosphotransferase enzyme I. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine. -!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. O31458 O31458 3.5.99.6 Glucosamine-6-phosphate deaminase. GlcN6P deaminase. Glucosamine phosphate deaminase. Glucosamine-6-phosphate isomerase. Phosphoglucosamine isomerase. Phosphoglucosaminisomerase. Alpha-D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). -!- Isomerization of the aldose-ketose type converts the -CH(-NH(2))-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH(2)-OH, forming 2-deoxy-2-imino-D-arabino-hexitol which then hydrolyzes to yield fructose 6-phosphate and ammonia. -!- N-acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme. -!- Formerly EC 5.3.1.10. O31544 O31544 3.2.2.21 DNA-3-methyladenine glycosylase II. DNA glycosidase II. DNA-3-methyladenine glycosidase II. Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine. O31611 O31611 2.7.6.5 GTP diphosphokinase. GTP pyrophosphokinase. Guanosine 3',5'-polyphosphate synthase. ppGpp synthetase I. Stringent factor. ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. -!- GDP can also act as acceptor. O31612 O31612 2.7.1.23 NAD(+) kinase. DPN kinase. ATP + NAD(+) = ADP + NADP(+). O31618 O31618 2.8.1.10 Thiazole synthase. 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur- carrier protein ThiS] = 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- ylidene)ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H(2)O. -!- H(2)S can provide the sulfur in vitro. -!- Part of the pathway for thiamine biosynthesis. O31644 O31644 2.7.1.191 Protein-N(pi)-phosphohistidine--D-mannose phosphotransferase. Mannose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L- histidine + D-mannose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. O31645 O31645 2.7.1.191 Protein-N(pi)-phosphohistidine--D-mannose phosphotransferase. Mannose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L- histidine + D-mannose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. O31646 O31646 5.3.1.8 Mannose-6-phosphate isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphomannoisomerase. Phosphomannose isomerase. D-mannose 6-phosphate = D-fructose 6-phosphate. Zn(2+). O31662 O31662 5.3.1.23 S-methyl-5-thioribose-1-phosphate isomerase. 1-phospho-5'-S-methylthioribose isomerase. 1-PMTR isomerase. 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase. 5-methylthioribose-1-phosphate isomerase. Methylthioribose 1-phosphate isomerase. MTR-1-P isomerase. S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate aldose-ketose-isomerase. S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol-isomerase. S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose-isomerase. S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate. O31663 O31663 2.7.1.100 S-methyl-5-thioribose kinase. 5-methylthioribose kinase. Methylthioribose kinase. MTR kinase. ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate. -!- Also acts, more slowly, on CTP. O31666 O31666 5.3.2.5 2,3-diketo-5-methylthiopentyl-1-phosphate enolase. DK-MTP-1-P enolase. RuBisCO-like protein. 5-(methylthio)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylthio)-3- oxopent-1-enyl phosphate. -!- The enzyme participates in the methionine salvage pathway in Bacillus subtilis. -!- In some species a single bifunctional enzyme, EC 3.1.3.77, catalyzes both this reaction and that of EC 3.1.3.87. -!- Formerly EC 5.3.2.n1. O31669 O31669 1.13.11.53 Acireductone dioxygenase (Ni(2+)-requiring). 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase. Acireductone dioxygenase. ARD. E-2. 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O(2) = 3-(methylthio)propanoate + formate + CO. Ni(2+). -!- If Fe(2+) is bound instead of Ni(2+), the reaction catalyzed by EC 1.13.11.54 occurs instead. -!- The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC 8724 is involved in the methionine salvage pathway. O31669 O31669 1.13.11.54 Acireductone dioxygenase (Fe(2+)-requiring). 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase. Acireductone dioxygenase. ARD'. E-2'. 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O(2) = 4-(methylthio)-2- oxobutanoate + formate. Fe(2+). -!- If Ni(2+) is bound instead of Fe(2+), the reaction catalyzed by EC 1.13.11.53 occurs instead. -!- The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC 8724 is involved in the methionine salvage pathway. O31741 O31741 2.1.1.228 tRNA (guanine(37)-N(1))-methyltransferase. Transfer RNA (m(1)G(37)) methyltransferase. tRNA (m(1)G(37)) methyltransferase. tRNA-(N(1)G37) methyltransferase. S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. -!- This enzyme is important for the maintenance of the correct reading frame during translation. -!- Unlike TrmD from Escherichia coli, which recognizes the G(36)pG(37) motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37. -!- Formerly EC 2.1.1.31. O31749 O31749 2.7.4.22 UMP kinase. UMP-kinase. UMPK. Uridine monophosphate kinase. Uridylate kinase. ATP + UMP = ADP + UDP. -!- Strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme EC 2.7.4.14 for the same purpose. -!- Subject of feedback regulation, being inhibited by UTP and activated by GTP. O31777 O31777 2.3.1.47 8-amino-7-oxononanoate synthase. 7-KAP synthetase. 7-keto-8-aminopelargonic acid synthetase. 8-amino-7-ketopelargonate synthase. AONS. Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein]. Pyridoxal 5'-phosphate. -!- The enzyme catalyzes the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis. -!- Pimeloyl-CoA can be used with lower efficiency. O31875 O31875 1.17.4.1 Ribonucleoside-diphosphate reductase. Ribonucleotide reductase. 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Fe(3+) or adenosylcob(III)alamin or Mn(2+). -!- This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. -!- There are three types of this enzyme differing in their cofactors. -!- Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. -!- In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6 and EC 1.17.4.2. O32033 O32033 2.7.1.48 Uridine kinase. Uridine monophosphokinase. ATP + uridine = ADP + UMP. -!- Cytidine can act as acceptor. -!- GTP and ITP can act as donors. O32038 O32038 6.1.1.23 Aspartate--tRNA(Asn) ligase. Nondiscriminating aspartyl-tRNA synthetase. ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx). -!- When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12. -!- It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn). -!- This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. -!- This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon). -!- The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn). O32039 O32039 6.1.1.21 Histidine--tRNA ligase. Histidine translase. Histidyl-tRNA synthetase. ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). O32053 O32053 2.4.2.29 tRNA-guanine(34) transglycosylase. Guanine insertion enzyme. Q-insertase. Queuine tRNA-ribosyltransferase. Queuine(34) transfer ribonucleate ribosyltransferase. TGT. tRNA guanine(34) transglycosidase. tRNA transglycosylase. (1) Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. (2) Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine(34) in tRNA + guanine. -!- Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. -!- In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. -!- In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ(1), which is ultimately modified to queuine. -!- The eubacterial enzyme can also use an earlier intermediate, preQ(0), to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn). -!- This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway. O32129 O32129 2.8.1.8 Lipoyl synthase. Lipoate synthase. [Protein]-N(6)-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S](2+) cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H(+) = [protein]-N(6)-((R)-dihydrolipoyl)-L- lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe(3+) + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin. Iron-sulfur. -!- This enzyme catalyzes the final step in the de novo biosynthesis of the lipoyl cofactor, the attachment of two sulfhydryl groups to C(6) and C(8) of a pendant octanoyl chain. -!- It is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (S-adenosylmethionine) by the addition of an electron from an iron-sulfur center. -!- The enzyme contains two [4Fe-4S] clusters. -!- The first cluster produces the radicals, which are converted into 5'-deoxyadenosine when they abstract hydrogen atoms from C(6) and C(8), respectively, leaving reactive radicals at these positions that interact with sulfur atoms within the second (auxiliary) cluster. -!- Having donated two sulfur atoms, the auxiliary cluster is degraded during catalysis, but is regenerated immediately by the transfer of a new cluster from iron-sulfur cluster carrier proteins. -!- Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. -!- Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). -!- An alternative lipoylation pathway involves EC 6.3.1.20, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs). O32144 O32144 1.17.1.4 Xanthine dehydrogenase. NAD-xanthine dehydrogenase. Xanthine oxidoreductase. Xanthine-NAD oxidoreductase. Xanthine/NAD(+) oxidoreductase. Xanthine + NAD(+) + H(2)O = urate + NADH. FAD; Iron-sulfur; Mo cation. -!- Acts on a variety of purines and aldehydes, including hypoxanthine. -!- The mammalian enzyme can also convert all-trans retinol to all-trans- retinoate, while the substrate is bound to a retinoid-binding protein. -!- The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum center. -!- The mammallian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). -!- During purification the enzyme is largely converted to an O(2)- dependent form, EC 1.17.3.2. -!- The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion. -!- The conversion can also occur in vivo. -!- Formerly EC 1.2.1.37 and EC 1.1.1.204. O32164 O32164 2.8.1.7 Cysteine desulfurase. Cysteine desulfurylase. L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. Pyridoxal 5'-phosphate. -!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. O32178 O32178 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase. Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase. (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. -!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211). O32213 O32213 1.8.1.2 Assimilatory sulfite reductase (NADPH). Sulfite reductase (NADPH). H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. FAD; FMN; Iron-sulfur; Siroheme. -!- The enzyme, which catalyzes the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. -!- Different from EC 1.8.99.5, which is involved in prokaryotic sulfur- based energy metabolism. -!- Formerly EC 1.8.99.1. O32224 O32224 1.7.1.17 FMN-dependent NADH-azoreductase. Anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH. FMN. -!- The enzyme catalyzes the reductive cleavage of an azo bond in aromatic azo compounds to form the corresponding amines. -!- Does not accept NADPH. -!- Cf. EC 1.7.1.6. O32231 O32231 3.1.13.1 Exoribonuclease II. Ribonuclease II. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. -!- Preference for single-stranded RNA. -!- The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5. -!- Similar enzymes: RNase Q, RNase BN, RNase PIII, RNase Y. -!- Formerly EC 3.1.4.20. O32264 O32264 1.1.1.215 Gluconate 2-dehydrogenase. 2-keto-D-gluconate reductase. 2-ketogluconate reductase. D-gluconate + NADP(+) = 2-dehydro-D-gluconate + NADPH. -!- Also acts on L-idonate, D-galactonate and D-xylonate. O33289 O33289 2.3.1.1 Amino-acid N-acetyltransferase. N-acetylglutamate synthase. Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. -!- Also acts with L-aspartate and, more slowly, with some other amino acids. O33768 O33768 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). O33770 O33770 2.6.1.9 Histidinol-phosphate transaminase. Histidinol-phosphate aminotransferase. Imidazole acetol-phosphate transaminase. Imidazolylacetolphosphate aminotransferase. L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. Pyridoxal 5'-phosphate. O33775 O33775 1.1.1.23 Histidinol dehydrogenase. L-histidinol + H(2)O + 2 NAD(+) = L-histidine + 2 NADH. -!- Also oxidizes L-histidinal. -!- The Neurospora enzyme also catalyzes the reactions of EC 3.5.4.19 and EC 3.6.1.31. O33780 O33780 6.1.1.11 Serine--tRNA ligase. Serine translase. SerRS. Seryl-transfer ribonucleate synthetase. Seryl-transfer ribonucleic acid synthetase. Seryl-transfer RNA synthetase. Seryl-tRNA synthetase. (1) ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). (2) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). -!- This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1. O34153 O34153 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. O34154 O34154 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. O34206 O34206 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. O34303 O34303 3.1.21.4 Type II site-specific deoxyribonuclease. Type II restriction enzyme. Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Mg(2+). -!- Large group of enzymes which recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition site. -!- See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ O34324 O34324 1.8.1.4 Dihydrolipoyl dehydrogenase. Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. FAD. -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3. O34328 O34328 2.7.4.8 Guanylate kinase. Deoxyguanylate kinase. GMP kinase. Guanosine monophosphate kinase. ATP + GMP = ADP + GDP. -!- dGMP can also act as acceptor. -!- dATP can act as donor. O34347 O34347 6.3.4.5 Argininosuccinate synthase. Arginine succinate synthetase. Argininosuccinate synthetase. Citrulline--aspartate ligase. ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate. O34425 O34425 1.2.1.59 Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating). NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase (NAD(P)(+)). Triosephosphate dehydrogenase (NAD(P)). D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D- glyceroyl phosphate + NAD(P)H. -!- NAD(+) and NADP(+) can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 and EC 1.2.1.13, which are NAD(+)- and NADP(+)- dependent, respectively. O34443 O34443 2.4.2.7 Adenine phosphoribosyltransferase. AMP diphosphorylase. AMP pyrophosphorylase. APRT. Transphosphoribosidase. AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. -!- 5-amino-4-imidazolecarboxamide can replace adenine. O34499 O34499 3.1.1.31 6-phosphogluconolactonase. 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-phospho-D-gluconate. O34507 O34507 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. O34529 O34529 2.7.1.11 6-phosphofructokinase. Phosphofructokinase I. Phosphohexokinase. ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. -!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. -!- UTP, CTP and ITP can act as donors. -!- Not identical with EC 2.7.1.105. O34660 O34660 1.2.1.3 Aldehyde dehydrogenase (NAD(+)). An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH. -!- Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. -!- Formerly EC 1.1.1.70. O34714 O34714 4.1.1.2 Oxalate decarboxylase. Oxalate carboxy-lyase. Oxalate = formate + CO(2). Mn(2+). O34764 O34764 2.7.7.4 Sulfate adenylyltransferase. ATP-sulfurylase. Sulfate adenylate transferase. Sulfurylase. ATP + sulfate = diphosphate + adenylyl sulfate. -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. O34788 O34788 1.1.1.4 (R,R)-butanediol dehydrogenase. (R)-2,3-butanediol dehydrogenase. (R)-diacetyl reductase. 1-amino-2-propanol dehydrogenase. 1-amino-2-propanol oxidoreductase. 2,3-butanediol dehydrogenase. Aminopropanol oxidoreductase. Butylene glycol dehydrogenase. Butyleneglycol dehydrogenase. D-(-)-butanediol dehydrogenase. D-1-amino-2-propanol dehydrogenase. D-1-amino-2-propanol:NAD(2) oxidoreductase. D-aminopropanol dehydrogenase. D-butanediol dehydrogenase. Diacetyl (acetoin) reductase. (R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH. -!- Also converts diacetyl into acetoin with NADH as reductant. O34824 O34824 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. O34872 O34872 4.2.1.1 Carbonic anhydrase. Carbonate dehydratase. Carbonate hydro-lyase. Carbonic dehydratase. H(2)CO(3) = CO(2) + H(2)O. Zn(2+). -!- The enzyme catalyzes the reversible hydration of gaseous CO(2) to carbonic acid, which spontaneously converts to hydrogencarbonate under neutral pH. -!- It is widespread and found in archaea, bacteria, and eukaryotes. -!- Three distinct classes exist, and appear to have evolved independently. O34909 O34909 3.5.4.2 Adenine deaminase. Adenase. Adenine aminase. Adenine + H(2)O = hypoxanthine + NH(3). O34962 O34962 1.1.1.38 Malate dehydrogenase (oxaloacetate-decarboxylating). Malic enzyme. NAD-malic enzyme. Pyruvic-malic carboxylase. (1) (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. (2) Oxaloacetate = pyruvate + CO(2). -!- Unlike EC 1.1.1.39, this enzyme can also decarboxylate oxaloacetate, cf. EC 1.1.1.40. O34981 O34981 2.3.1.89 Tetrahydrodipicolinate N-acetyltransferase. Tetrahydrodipicolinate acetylase. Acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + L-2-acetamido-6-oxoheptanedioate. O35033 O35033 4.1.1.36 Phosphopantothenoylcysteine decarboxylase. N-((R)-4'-phosphopantothenoyl)-L-cysteine carboxy-lyase. N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO(2). FMN. O35033 O35033 6.3.2.5 Phosphopantothenate--cysteine ligase (CTP). Phosphopantothenate--cysteine ligase. Phosphopantothenoylcysteine synthetase. CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine. O52631 O52631 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. O52632 O52632 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. O53181 O53181 1.2.7.3 2-oxoglutarate synthase. 2-ketoglutarate ferredoxin oxidoreductase. 2-oxoglutarate ferredoxin oxidoreductase. Alpha-ketoglutarate synthase. Alpha-ketoglutarate-ferredoxin oxidoreductase. KGOR. 2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). Iron-sulfur; Thiamine diphosphate. -!- Highly specific for 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.7. -!- Formerly EC 1.2.7.9. O53203 O53203 1.4.1.2 Glutamate dehydrogenase. Glutamic dehydrogenase. L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH. O53493 O53493 2.3.1.269 Apolipoprotein N-acyltransferase. A phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L- cysteine = a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2- diacyl-sn-glyceryl-L-cysteine. -!- This bacterial enzyme transfers a fatty acid from a membrane phospholipid to form an amide linkage with the N-terminal cysteine residue of apolipoproteins, generating a triacylated molecule. O53493 O53493 2.4.1.83 Dolichyl-phosphate beta-D-mannosyltransferase. Dolichol-phosphate mannose synthase. Dolichol-phosphate mannosyltransferase. Mannosylphosphodolichol synthase. Mannosylphosphoryldolichol synthase. GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate. -!- Acts only on long-chain polyprenyl phosphates and alpha- dihydropolyprenyl phosphates, larger than C(35). O53512 O53512 2.5.1.54 3-deoxy-7-phosphoheptulonate synthase. 2-dehydro-3-deoxy-phosphoheptonate aldolase. 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). D-erythrose-4-phosphate-lyase. D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating). DAH7-P synthase. DAHP synthase. Deoxy-D-arabino-heptulosonate-7-phosphate synthetase. DHAP synthase. DS-Co. DS-Mn. KDPH synthase. KDPH synthetase. Phospho-2-dehydro-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptanoate aldolase. Phospho-2-keto-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptonic aldolase. Phospho-2-oxo-3-deoxyheptonate aldolase. Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D- arabino-hept-2-ulosonate 7-phosphate + phosphate. -!- Formerly EC 4.1.2.15. O53521 O53521 6.2.1.3 Long-chain-fatty-acid--CoA ligase. Acyl-activating enzyme. Acyl-CoA synthetase. Fatty acid thiokinase (long chain). Lignoceroyl-CoA synthase. ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. -!- Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. -!- The liver enzyme acts on acids from C(6) to C(20); that from brain shows high activity up to C(24). O53857 O53857 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. O69670 O69670 3.5.1.118 Gamma-glutamyl hercynylcysteine S-oxide hydrolase. Gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H(2)O = S-(hercyn- 2-yl)-L-cysteine S-oxide + L-glutamate. -!- The enzyme is part of the biosynthesis pathway of ergothioneine in mycobacteria. P00350 P00350 1.1.1.44 Phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating). 6-phosphogluconic carboxylase. 6-phosphogluconic dehydrogenase. 6PGD. Phosphogluconic acid dehydrogenase. 6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH. -!- The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. -!- Highly specific for NADP(+). -!- Cf. EC 1.1.1.343. P00363 P00363 1.3.5.4 Fumarate reductase (quinol). Fumarate reductase (menaquinone). Succinate dehydrogenase (menaquinone). Succinate + a quinone = fumarate + a quinol. -!- The enzyme, which is found in anaerobic and facultative organisms such as bacteria, parasitic helminthes, and lower marine organisms, utilizes low potential quinols, such as menaquinol and rhodoquinol, to reduce fumarate as the final step of an anaerobic respiratory chain. -!- The enzyme is known as complex II of the electron transfer chain, similarly to EC 1.3.5.1, to which it is closely related. P00370 P00370 1.4.1.4 Glutamate dehydrogenase (NADP(+)). Glutamic dehydrogenase. L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate + NH(3) + NADPH. P00448 P00448 1.15.1.1 Superoxide dismutase. 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Fe cation or Mn(2+) or (Zn(2+) and Cu cation). P00509 P00509 2.6.1.1 Aspartate transaminase. Aspartate aminotransferase. Glutamic--aspartic transaminase. Glutamic--oxaloacetic transaminase. Transaminase A. L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Pyridoxal 5'-phosphate. -!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. -!- This activity can be formed from EC 2.6.1.57 by controlled proteolysis. P00550 P00550 2.7.1.197 Protein-N(pi)-phosphohistidine--D-mannitol phosphotransferase. D-mannitol PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-mannitol(Side 1) = [protein]-L- histidine + D-mannitol 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate--protein phosphotransferase). -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P00562 P00562 1.1.1.3 Homoserine dehydrogenase. L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H. -!- The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+). -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4. P00562 P00562 2.7.2.4 Aspartate kinase. Aspartokinase. ATP + L-aspartate = ADP + 4-phospho-L-aspartate. -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3. -!- This is also the case for two of the four isoenzymes in Arabidopsis thaliana. -!- The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction. P00582 P00582 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P00634 P00634 3.1.3.1 Alkaline phosphatase. Alkaline phosphomonoesterase. Glycerophosphatase. Phosphomonoesterase. A phosphate monoester + H(2)O = an alcohol + phosphate. Mg(2+); Zn(2+). -!- Active at a high pH optimum. -!- Wide specificity. -!- Also catalyzes transphosphorylations. -!- Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1). P00811 P00811 3.5.2.6 Beta-lactamase. Cephalosporinase. Penicillinase. A beta-lactam + H(2)O = a substituted beta-amino acid. Zn(2+). -!- Zinc is only requires in class-B enzymes. -!- A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. -!- Formerly EC 3.5.2.8. P00864 P00864 4.1.1.31 Phosphoenolpyruvate carboxylase. PEP carboxylase. PEPCase. Phosphoenolpyruvic carboxylase. Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-). -!- This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. -!- The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate. P00909 P00909 4.1.1.48 Indole-3-glycerol-phosphate synthase. Indoleglycerol phosphate synthetase. 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C- (3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. -!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.3.27, EC 4.2.1.20 and EC 5.3.1.24). P00909 P00909 5.3.1.24 Phosphoribosylanthranilate isomerase. N-(5'-phosphoribosyl)anthranilate isomerase. PRAI. N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate. -!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 4.2.1.20). P00936 P00936 4.6.1.1 Adenylate cyclase. 3',5'-cyclic AMP synthetase. Adenyl cyclase. Adenylyl cyclase. ATP pyrophosphate-lyase. ATP = 3',5'-cyclic AMP + diphosphate. -!- Also acts on dATP to form 3',5'-cyclic dAMP. -!- Requires pyruvate. -!- Activated by NAD(+) in presence of EC 2.4.2.31. P00946 P00946 5.3.1.8 Mannose-6-phosphate isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphomannoisomerase. Phosphomannose isomerase. D-mannose 6-phosphate = D-fructose 6-phosphate. Zn(2+). P00954 P00954 6.1.1.2 Tryptophan--tRNA ligase. L-tryptophan-tRNA(Trp) ligase (AMP-forming). TrpRS. Tryptophan translase. Tryptophanyl ribonucleic synthetase. Tryptophanyl-transfer ribonucleate synthetase. Tryptophanyl-transfer ribonucleic acid synthetase. Tryptophanyl-transfer ribonucleic synthetase. Tryptophanyl-transfer RNA synthetase. Tryptophanyl-tRNA synthase. Tryptophanyl-tRNA synthetase. ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl- tRNA(Trp). P00956 P00956 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). P00959 P00959 6.1.1.10 Methionine--tRNA ligase. Methionine translase. Methionyl-transfer ribonucleate synthetase. Methionyl-transfer ribonucleic acid synthetase. Methionyl-transfer RNA synthetase. Methionyl-tRNA synthetase. MetRS. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl- tRNA(Met). -!- In those organisms producing N-formylmethionyl-tRNA(fMet) for translation initiation, this enzyme also recognizes the initiator tRNA(fMet) and catalyzes the formation of L-methionyl-tRNA(fMet), the substrate for EC 2.1.2.9. P00961 P00961 6.1.1.14 Glycine--tRNA ligase. Glycyl translase. Glycyl-tRNA synthetase. ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). P00968 P00968 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. P03018 P03018 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P04036 P04036 1.17.1.8 4-hydroxy-tetrahydrodipicolinate reductase. Dihydrodipicolinate reductase. (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H. -!- Studies of the enzyme from the bacterium Escherichia coli have shown that the enzyme accepts (2S,4S)-4-hydroxy-2,3,4,5- tetrahydrodipicolinate and not (S)-2,3-dihydrodipicolinate as originally thought. -!- Formerly EC 1.3.1.26. P04042 P04042 3.1.1.61 Protein-glutamate methylesterase. CheB methylesterase. Chemotaxis-specific methylesterase. Methyl-accepting chemotaxis protein methyl-esterase. Methylesterase CheB. PME. Protein carboxyl methylesterase. Protein methyl-esterase. Protein methylesterase. Protein L-glutamate O(5)-methyl ester + H(2)O = protein L-glutamate + methanol. -!- Hydrolyzes the products of EC 2.1.1.77, EC 2.1.1.78, EC 2.1.1.80 and EC 2.1.1.100. P04042 P04042 3.5.1.44 Protein-glutamine glutaminase. Glutaminylpeptide glutaminase. Peptidoglutaminase II. Protein L-glutamine + H(2)O = protein L-glutamate + NH(3). -!- Specific for the hydrolysis of the gamma-amide of glutamine substituted at the carboxyl position or both the alpha-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L- glutaminylglycine. P04079 P04079 6.3.5.2 GMP synthase (glutamine-hydrolyzing). GMP synthetase (glutamine-hydrolyzing). ATP + XMP + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate. -!- Involved in the de novo biosynthesis of guanosine nucleotides. -!- An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. -!- The enzyme can catalyze the second reaction alone in the presence of ammonia. -!- Formerly EC 6.3.4.1. P04805 P04805 6.1.1.17 Glutamate--tRNA ligase. Glutamic acid translase. Glutamyl-tRNA synthetase. ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). P04951 P04951 2.7.7.38 3-deoxy-manno-octulosonate cytidylyltransferase. CMP-2-keto-3-deoxyoctulosonic acid synthetase. CMP-3-deoxy-D-manno-octulosonate diphosphorylase. CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase. CMP-KDO synthetase. CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno- octulosonate. P04990 P04990 4.2.3.1 Threonine synthase. O-phospho-L-homoserine + H(2)O = L-threonine + phosphate. Pyridoxal 5'-phosphate. -!- Formerly EC 4.2.99.2. P05055 P05055 2.7.7.8 Polyribonucleotide nucleotidyltransferase. Polynucleotide phosphorylase. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. -!- ADP, IDP, GDP, UDP and CDP can act as donors. P05459 P05459 1.1.1.290 4-phosphoerythronate dehydrogenase. 4-O-phosphoerythronate dehydrogenase. 4PE dehydrogenase. Erythronate-4-phosphate dehydrogenase. 4-phospho-D-erythronate + NAD(+) = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + NADH. NAD(+). -!- This enzyme catalyzes a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. -!- The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD(+). -!- In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyzes the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)- hydroxy acid. -!- Cf. EC 1.1.1.399. P05645 P05645 1.1.1.85 3-isopropylmalate dehydrogenase. Beta-IPM dehydrogenase. Beta-isopropylmalate dehydrogenase. IMDH. (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH. P05652 P05652 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P05653 P05653 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P05654 P05654 2.1.3.2 Aspartate carbamoyltransferase. Aspartate transcarbamylase. ATCase. Carbamylaspartotranskinase. Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. P05793 P05793 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. P06612 P06612 5.6.2.2 DNA topoisomerase. DNA topoisomerase I. Nicking-closing enzyme. Omega-protein. Relaxing enzyme. Swivelase. Type I DNA topoisomerase. Untwisting enzyme. ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. -!- These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.6.2.3. -!- Formerly EC 5.99.1.2. P06959 P06959 2.3.1.12 Dihydrolipoyllysine-residue acetyltransferase. Acetyl-CoA:dihydrolipoamide S-acetyltransferase. Dihydrolipoamide S-acetyltransferase. Dihydrolipoate acetyltransferase. Dihydrolipoic transacetylase. Dihydrolipoyl acetyltransferase. Lipoate acetyltransferase. Lipoate transacetylase. Lipoic acetyltransferase. Lipoic acid acetyltransferase. Lipoic transacetylase. Lipoylacetyltransferase. Thioltransacetylase A. Transacetylase X. Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine. -!- A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A. P06999 P06999 2.7.1.11 6-phosphofructokinase. Phosphofructokinase I. Phosphohexokinase. ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. -!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. -!- UTP, CTP and ITP can act as donors. -!- Not identical with EC 2.7.1.105. P07003 P07003 1.2.5.1 Pyruvate dehydrogenase (quinone). Pyruvate dehydrogenase. Pyruvate dehydrogenase (cytochrome). Pyruvate oxidase. Pyruvate + ubiquinone + H(2)O = acetate + CO(2) + ubiquinol. FAD. -!- This bacterial enzyme is located on the inner surface of the cytoplasmic membrane and coupled to the respiratory chain via ubiquinone. -!- Does not accept menaquinone. -!- Activity is greatly enhanced by lipids. -!- Requires thiamine diphosphate. -!- The enzyme can also form acetoin. P07343 P07343 4.2.1.2 Fumarate hydratase. Fumarase. (S)-malate = fumarate + H(2)O. P07363 P07363 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P07639 P07639 4.2.3.4 3-dehydroquinate synthase. 3-dehydroquinate synthetase. 5-dehydroquinate synthase. 5-dehydroquinic acid synthetase. Dehydroquinate synthase. 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate. Cobalt cation; NAD(+). -!- The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products. -!- Formerly EC 4.6.1.3. P07650 P07650 2.4.2.4 Thymidine phosphorylase. Pyrimidine phosphorylase. Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. -!- In some tissues also catalyzes deoxyribosyltransferase reactions of the type catalyzed by EC 2.4.2.6. -!- Formerly EC 2.4.2.23. P08065 P08065 1.3.5.1 Succinate dehydrogenase (quinone). Succinate dehydrogenase (ubiquinone). Succinic dehydrogenase. Succinate + a quinone = fumarate + a quinol. FAD; Iron-sulfur. -!- The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. -!- It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). -!- In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. -!- Cf. EC 1.3.5.4. P08066 P08066 1.3.5.1 Succinate dehydrogenase (quinone). Succinate dehydrogenase (ubiquinone). Succinic dehydrogenase. Succinate + a quinone = fumarate + a quinol. FAD; Iron-sulfur. -!- The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. -!- It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). -!- In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. -!- Cf. EC 1.3.5.4. P08164 P08164 6.3.1.5 NAD(+) synthase. NAD(+) synthetase. ATP + deamido-NAD(+) + NH(3) = AMP + diphosphate + NAD(+). -!- L-glutamine also acts, more slowly, as amido-donor (cf. EC 6.3.5.1). P08178 P08178 6.3.3.1 Phosphoribosylformylglycinamidine cyclo-ligase. AIR synthase. AIR synthetase. AIRS. Phosphoribosyl-aminoimidazole synthetase. Phosphoribosylaminoimidazole synthetase. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. P08192 P08192 6.3.2.12 Dihydrofolate synthase. 7,8-dihydrofolate synthetase. DHFS. Dihydrofolate synthetase. H(2)-folate synthetase. ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8- dihydropteroylglutamate. -!- In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.17, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates. -!- In contrast, the activities are located on separate proteins in most eukaryotes studied to date. -!- This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa. P08192 P08192 6.3.2.17 Tetrahydrofolate synthase. Folate polyglutamate synthetase. Folylpoly(gamma-glutamate) synthase. Folylpoly-gamma-glutamate synthase. Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase. Folylpolyglutamate synthase. Folylpolyglutamate synthetase. Folylpolyglutamyl synthetase. Formyltetrahydropteroyldiglutamate synthetase. FPGS. N(10)-formyltetrahydropteroyldiglutamate synthetase. Tetrahydrofolate:L-glutamate gamma-ligase (ADP-forming). Tetrahydrofolylpolyglutamate synthase. ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). -!- In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.12, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates (H(4)folate). -!- In contrast, the activities are located on separate proteins in most eukaryotes studied to date. -!- In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast. -!- Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes. -!- As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C(1) metabolism. -!- The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates. P08200 P08200 1.1.1.42 Isocitrate dehydrogenase (NADP(+)). Dual-cofactor-specific isocitrate dehydrogenase. IDH. IDP. Isocitrate (NADP) dehydrogenase. Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Isocitrate dehydrogenase (NADP). Isocitrate dehydrogenase (NADP-dependent). NADP isocitric dehydrogenase. NADP(+)-ICDH. NADP(+)-IDH. NADP(+)-linked isocitrate dehydrogenase. NADP-dependent isocitrate dehydrogenase. NADP-dependent isocitric dehydrogenase. NADP-linked isocitrate dehydrogenase. NADP-specific isocitrate dehydrogenase. Oxalosuccinate decarboxylase. Oxalsuccinic decarboxylase. Triphosphopyridine nucleotide-linked isocitrate dehydrogenase- oxalosuccinate carboxylase. Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Mn(2+) or Mg(2+). -!- Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate. -!- In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. -!- The enzyme from some species can also use NAD(+) but much more slowly. P08312 P08312 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). P08400 P08400 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P08506 P08506 3.4.16.4 Serine-type D-Ala-D-Ala carboxypeptidase. D-alanyl-D-alanine carboxypeptidase. DD-peptidase. DD-transpeptidase. Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. -!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13. P08838 P08838 2.7.3.9 Phosphoenolpyruvate--protein phosphotransferase. Enzyme I of the phosphotransferase system. Phosphoenolpyruvate sugar phosphotransferase enzyme I. Phosphoenolpyruvate--protein phosphatase. Phosphopyruvate--protein factor phosphotransferase. Phosphopyruvate--protein phosphotransferase. Sugar--PEP phosphotransferase enzyme I. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine. -!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. P08839 P08839 2.7.3.9 Phosphoenolpyruvate--protein phosphotransferase. Enzyme I of the phosphotransferase system. Phosphoenolpyruvate sugar phosphotransferase enzyme I. Phosphoenolpyruvate--protein phosphatase. Phosphopyruvate--protein factor phosphotransferase. Phosphopyruvate--protein phosphotransferase. Sugar--PEP phosphotransferase enzyme I. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine. -!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. P08997 P08997 2.3.3.9 Malate synthase. Glyoxylate transacetase. Glyoxylate transacetylase. Glyoxylic transacetase. L-malate glyoxylate-lyase (CoA-acetylating). Malate condensing enzyme. Malate synthetase. Malic synthetase. Malic-condensing enzyme. Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA. -!- The enzyme catalyzes the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. -!- Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO(2). -!- Formerly EC 4.1.3.2. P09030 P09030 3.1.11.2 Exodeoxyribonuclease III. E.coli exonuclease III. Exonuclease III. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. -!- Preference for double-stranded DNA. -!- Has endonucleolytic activity near apurinic sites on DNA. -!- Similar enzyme: Haemophilus influenzae exonuclease. -!- Formerly EC 3.1.4.27. P09124 P09124 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. P09152 P09152 1.7.5.1 Nitrate reductase (quinone). Dissimilatory nitrate reductase. Nitrate reductase A. Nitrate reductase Z. Quinol-nitrate oxidoreductase. Quinol/nitrate oxidoreductase. Nitrate + a quinol = nitrite + a quinone + H(2)O. Heme; Iron-sulfur; Molybdopterin guanine dinucleotide. -!- A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits. P09169 P09169 3.4.23.49 Omptin. Outer membrane protein 3B. Protease A. Protease VII. Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. -!- Shows a preference for cleavage between consecutive basic amino acids, but is capable of cleavage when P1' is a non-basic residue. -!- Belongs to peptidase family A26. -!- Formerly EC 3.4.21.87. P09323 P09323 2.7.1.193 Protein-N(pi)-phosphohistidine--N-acetyl-D-glucosamine phosphotransferase. N-acetyl-D-glucosamine PTS permease. [Protein]-N(pi)-phospho-L-histidine + N-acetyl-D-glucosamine(Side 1) = [protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P09339 P09339 4.2.1.3 Aconitate hydratase. Aconitase. Cis-aconitase. Citrate hydro-lyase. Citrate(isocitrate) hydro-lyase. Citrate = isocitrate. Iron-sulfur. -!- Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. -!- The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. -!- Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3- tricarboxylate. -!- Formerly EC 4.2.1.4. P09373 P09373 2.3.1.54 Formate C-acetyltransferase. Pyruvate formate-lyase. Acetyl-CoA + formate = CoA + pyruvate. P09384 P09384 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P09546 P09546 1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenase. 1-pyrroline-5-carboxylate dehydrogenase. Delta(1)-pyrroline-5-carboxylate dehydrogenase. Pyrroline-5-carboxylate dehydrogenase. L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH. -!- This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. -!- (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. -!- In many bacterial species, both activities are carried out by a single bifunctional enzyme. -!- The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. -!- NADP(+) can also act as acceptor, but with lower activity. -!- Formerly EC 1.5.1.12. P09546 P09546 1.5.5.2 Proline dehydrogenase. L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol. FAD. -!- The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor. -!- In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88. -!- Both activities are carried out by the same enzyme in enterobacteria. -!- Formerly EC 1.5.99.8. P09835 P09835 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P09924 P09924 4.1.2.4 Deoxyribose-phosphate aldolase. 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase. Deoxyriboaldolase. Phosphodeoxyriboaldolase. 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. P0A252 P0A252 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0A2D9 P0A2D9 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0A435 P0A435 2.7.1.200 Protein-N(pi)-phosphohistidine--galactitol phosphotransferase. Galactitol PTS permease. [Protein]-N(pi)-phospho-L-histidine + galactitol(Side 1) = [protein]-L- histidine + galactitol 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P0A4S0 P0A4S0 4.2.1.8 Mannonate dehydratase. Altronate hydrolase. D-mannonate hydro-lyase. Mannonic hydrolase. D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H(2)O. P0A5S5 P0A5S5 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P0A6A3 P0A6A3 2.7.2.1 Acetate kinase. Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK. ATP + acetate = ADP + acetyl phosphate. Mg(2+). -!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. P0A6A5 P0A6A5 2.7.2.1 Acetate kinase. Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK. ATP + acetate = ADP + acetyl phosphate. Mg(2+). -!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. P0A6B7 P0A6B7 2.8.1.7 Cysteine desulfurase. Cysteine desulfurylase. L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. Pyridoxal 5'-phosphate. -!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. P0A6D7 P0A6D7 2.7.1.71 Shikimate kinase. ATP + shikimate = ADP + shikimate 3-phosphate. P0A6E4 P0A6E4 6.3.4.5 Argininosuccinate synthase. Arginine succinate synthetase. Argininosuccinate synthetase. Citrulline--aspartate ligase. ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate. P0A6F3 P0A6F3 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. P0A6F4 P0A6F4 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. P0A6G3 P0A6G3 3.5.1.42 Nicotinamide-nucleotide amidase. Beta-nicotinamide D-ribonucleotide + H(2)O = beta-nicotinate D-ribonucleotide + NH(3). -!- Also acts more slowly on beta-nicotinamide D-ribonucleoside. P0A6G9 P0A6G9 3.4.21.92 Endopeptidase Clp. Caseinolytic protease. Endopeptidase Ti. Protease Ti. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). -!- Belongs to peptidase family S14. P0A6I0 P0A6I0 2.7.4.25 (d)CMP kinase. dCMP kinase. Deoxycytidine monophosphokinase. Deoxycytidylate kinase. ATP + (d)CMP = ADP + (d)CDP. -!- The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. -!- Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22. -!- The enzyme phosphorylates dCMP nearly as well as it does CMP. P0A6K6 P0A6K6 5.4.2.7 Phosphopentomutase. Deoxyribomutase. Deoxyribose phosphomutase. Phosphodeoxyribomutase. Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. -!- Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D- ribose 5-phosphate. -!- Alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5- bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.6. P0A6L0 P0A6L0 4.1.2.4 Deoxyribose-phosphate aldolase. 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase. Deoxyriboaldolase. Phosphodeoxyriboaldolase. 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. P0A6P9 P0A6P9 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. P0A6Q1 P0A6Q1 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. P0A6Q2 P0A6Q2 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. P0A6Q3 P0A6Q3 4.2.1.59 3-hydroxyacyl-[acyl-carrier-protein] dehydratase. (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase. Beta-hydroxyoctanoyl thioester dehydratase. Beta-hydroxyoctanoyl-ACP-dehydrase. Beta-hydroxyoctanoyl-acyl carrier protein dehydrase. D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase. A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O. -!- This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- The enzyme uses fatty acyl thioesters of ACP in vivo. -!- Different forms of the enzyme may have preferences for substrates with different chain length. -!- For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. -!- Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14. -!- Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0). -!- FabZ, but not FabA, can also accept unsaturated substrates. -!- Formerly EC 4.2.1.58, EC 4.2.1.60 and EC 4.2.1.61. P0A6Q3 P0A6Q3 5.3.3.14 Trans-2-decenoyl-[acyl-carrier-protein] isomerase. Beta-hydroxydecanoyl thioester dehydrase. Trans-2,cis-3-decenoyl-ACP isomerase. Trans-2-decenoyl-ACP isomerase. Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier- protein]. -!- While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs. -!- ACP can be replaced by either CoA or N-acetylcysteamine thioesters. -!- The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis. P0A6T1 P0A6T1 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. P0A6T2 P0A6T2 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. P0A6T3 P0A6T3 2.7.1.6 Galactokinase. ATP + alpha-D-galactose = ADP + alpha-D-galactose 1-phosphate. -!- Part of the Leloir pathway for galactose metabolism. -!- The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-alpha-D-galactosamine. P0A6T5 P0A6T5 3.5.4.16 GTP cyclohydrolase I. GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate. -!- The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. -!- Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12. P0A6T8 P0A6T8 3.5.4.16 GTP cyclohydrolase I. GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate. -!- The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. -!- Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12. P0A6V3 P0A6V3 2.7.7.27 Glucose-1-phosphate adenylyltransferase. ADP-glucose diphosphorylase. ADP-glucose pyrophosphorylase. ADP-glucose synthase. ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose. P0A6V4 P0A6V4 2.7.7.27 Glucose-1-phosphate adenylyltransferase. ADP-glucose diphosphorylase. ADP-glucose pyrophosphorylase. ADP-glucose synthase. ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose. P0A6V5 P0A6V5 2.8.1.1 Thiosulfate sulfurtransferase. Rhodanese. Thiosulfate cyanide transsulfurase. Thiosulfate thiotransferase. Thiosulfate + cyanide = sulfite + thiocyanate. -!- A few other sulfur compounds can act as donors. P0A6W9 P0A6W9 6.3.2.2 Glutamate--cysteine ligase. Gamma-glutamyl-L-cysteine synthetase. Gamma-glutamylcysteine synthetase. ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L- cysteine. -!- Can use L-aminohexanoate in place of glutamate. P0A717 P0A717 2.7.6.1 Ribose-phosphate diphosphokinase. Phosphoribosyl diphosphate synthetase. Phosphoribosyl pyrophosphate synthetase. Ribose-phosphate pyrophosphokinase. ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. -!- dATP can also act as donor. P0A719 P0A719 2.7.6.1 Ribose-phosphate diphosphokinase. Phosphoribosyl diphosphate synthetase. Phosphoribosyl pyrophosphate synthetase. Ribose-phosphate pyrophosphokinase. ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. -!- dATP can also act as donor. P0A722 P0A722 2.3.1.129 Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase. Acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase. UDP-N-acetylglucosamine acyltransferase. (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D- glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)- N-acetyl-alpha-D-glucosamine. -!- Involved with EC 2.4.1.182 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli. P0A745 P0A745 1.8.4.11 Peptide-methionine (S)-S-oxide reductase. Methionine S-oxide reductase. Methionine S-oxide reductase (S-form oxidizing). Methionine sulfoxide reductase. Methionine sulfoxide reductase A. Methionine sulphoxide reductase A. Peptide Met(O) reductase. Peptide methionine sulfoxide reductase. (1) Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (S)-S-oxide + thioredoxin. (2) L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S- oxide + thioredoxin. -!- The reaction occurs in the reverse direction to that shown above. -!- Exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid. -!- On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly. -!- Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. -!- The reaction proceeds via a sulfenic-acid intermediate. -!- Formerly EC 1.8.4.6. P0A746 P0A746 1.8.4.12 Peptide-methionine (R)-S-oxide reductase. Methionine S-oxide reductase. Methionine S-oxide reductase (R-form oxidizing). Methionine sulfoxide reductase. Methionine sulfoxide reductase B. Selenoprotein R. Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (R)-S-oxide + thioredoxin. Se(2+); Zn(2+). -!- The reaction occurs in the reverse direction to that shown above. -!- Exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide. -!- While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater. -!- Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. -!- The reaction proceeds via a sulfenic-acid intermediate. -!- For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well. P0A759 P0A759 3.5.99.6 Glucosamine-6-phosphate deaminase. GlcN6P deaminase. Glucosamine phosphate deaminase. Glucosamine-6-phosphate isomerase. Phosphoglucosamine isomerase. Phosphoglucosaminisomerase. Alpha-D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). -!- Isomerization of the aldose-ketose type converts the -CH(-NH(2))-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH(2)-OH, forming 2-deoxy-2-imino-D-arabino-hexitol which then hydrolyzes to yield fructose 6-phosphate and ammonia. -!- N-acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme. -!- Formerly EC 5.3.1.10. P0A761 P0A761 5.1.3.9 N-acylglucosamine-6-phosphate 2-epimerase. Acylglucosamine phosphate 2-epimerase. Acylglucosamine-6-phosphate 2-epimerase. Acylmannosamine phosphate 2-epimerase. N-acetylglucosmamine 6-phosphate 2-epimerase. N-acetylmannosamine-6-phosphate 2-epimerase. N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate. P0A763 P0A763 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. P0A764 P0A764 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. P0A796 P0A796 2.7.1.11 6-phosphofructokinase. Phosphofructokinase I. Phosphohexokinase. ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. -!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. -!- UTP, CTP and ITP can act as donors. -!- Not identical with EC 2.7.1.105. P0A797 P0A797 2.7.1.11 6-phosphofructokinase. Phosphofructokinase I. Phosphohexokinase. ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. -!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. -!- UTP, CTP and ITP can act as donors. -!- Not identical with EC 2.7.1.105. P0A799 P0A799 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. P0A7A9 P0A7A9 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P0A7B0 P0A7B0 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P0A7B5 P0A7B5 2.7.2.11 Glutamate 5-kinase. Gamma-glutamyl kinase. ATP + L-glutamate = ADP + L-glutamate 5-phosphate. -!- The product rapidly cyclizes to 5-oxoproline and phosphate. P0A7C6 P0A7C6 3.4.13.21 Dipeptidase E. Aspartyl dipeptidase. PepE gene product (Salmonella typhimurium). Peptidase E. Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides. -!- A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH(2) and Asp-Phe-OMe are hydrolyzed somewhat more slowly than dipeptides with free C-termini. -!- No peptide larger than a C-blocked dipeptide is known to be a substrate. -!- Asp-NH-Np is hydrolyzed and is a convenient substrate for routine assay. -!- The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride. -!- Belongs to peptidase family S51. P0A7C7 P0A7C7 3.4.13.21 Dipeptidase E. Aspartyl dipeptidase. PepE gene product (Salmonella typhimurium). Peptidase E. Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides. -!- A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH(2) and Asp-Phe-OMe are hydrolyzed somewhat more slowly than dipeptides with free C-termini. -!- No peptide larger than a C-blocked dipeptide is known to be a substrate. -!- Asp-NH-Np is hydrolyzed and is a convenient substrate for routine assay. -!- The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride. -!- Belongs to peptidase family S51. P0A7D4 P0A7D4 6.3.4.4 Adenylosuccinate synthase. Adenylosuccinate synthetase. IMP--aspartate ligase. Succinoadenylic kinosynthetase. GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)- AMP. P0A7D9 P0A7D9 6.3.2.6 Phosphoribosylaminoimidazolesuccinocarboxamide synthase. 4-((N-succinylamino)carbonyl)-5-aminoimidazole ribonucleotide synthetase. 4-(N-succinocarboxamide)-5-aminoimidazole synthetase. 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase. Phosphoribosylaminoimidazole-succinocarboxamide synthase. Phosphoribosylaminoimidazole-succinocarboxamide synthetase. Phosphoribosylaminoimidazolesuccinocarboxamide synthetase. SAICAR synthase. SAICAR synthetase. SAICARs. ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate. -!- Forms part of the purine biosynthesis pathway. P0A7E5 P0A7E5 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. P0A7E8 P0A7E8 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. P0A7F8 P0A7F8 4.1.1.50 Adenosylmethionine decarboxylase. S-adenosyl-L-methionine carboxy-lyase. S-adenosyl-L-methionine decarboxylase. S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2). Pyruvate. P0A7I9 P0A7I9 3.5.4.25 GTP cyclohydrolase II. GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D- ribosylamino)pyrimidine + diphosphate. -!- Two C-N bonds are hydrolyzed, releasing formate, with simultaneous removal of the terminal diphosphate. P0A7Y0 P0A7Y0 3.1.26.3 Ribonuclease III. Ribonuclease 3. RNase III. Endonucleolytic cleavage to 5'-phosphomonoester. -!- An endoribonuclease that cleaves double-stranded RNA molecules. -!- The cleavage can be either a single-stranded nick or double-stranded break in the RNA, depending in part upon the degree of base-pairing in the region of the cleavage site. -!- Specificity is conferred by negative determinants, i.e., the presence of certain Watson-Crick base-pairs at specific positions that strongly inhibit cleavage. -!- RNase III is involved in both rRNA processing and mRNA processing and decay. P0A7Z0 P0A7Z0 5.3.1.6 Ribose-5-phosphate isomerase. 5-phosphoribose isomerase. D-ribose-5-phosphate ketol-isomerase. Phosphopentoseisomerase. Phosphopentosisomerase. Phosphoriboisomerase. Ribose 5-phosphate epimerase. Ribose phosphate isomerase. D-ribose 5-phosphate = D-ribulose 5-phosphate. -!- Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate. P0A7Z2 P0A7Z2 5.3.1.6 Ribose-5-phosphate isomerase. 5-phosphoribose isomerase. D-ribose-5-phosphate ketol-isomerase. Phosphopentoseisomerase. Phosphopentosisomerase. Phosphoriboisomerase. Ribose 5-phosphate epimerase. Ribose phosphate isomerase. D-ribose 5-phosphate = D-ribulose 5-phosphate. -!- Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate. P0A7Z4 P0A7Z4 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A7Z6 P0A7Z6 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A7Z9 P0A7Z9 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A812 P0A812 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P0A817 P0A817 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. P0A825 P0A825 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. P0A827 P0A827 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. P0A836 P0A836 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P0A838 P0A838 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P0A839 P0A839 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P0A850 P0A850 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. P0A851 P0A851 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. P0A853 P0A853 4.1.99.1 Tryptophanase. L-tryptophan indole-lyase. TNase. L-tryptophan + H(2)O = indole + pyruvate + NH(3). K(+); Pyridoxal 5'-phosphate. -!- The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- Also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine and other 3-substituted amino acids. P0A858 P0A858 5.3.1.1 Triose-phosphate isomerase. Phosphotriose isomerase. Triose phosphoisomerase. Triosephosphate isomerase. Triosephosphate mutase. D-glyceraldehyde 3-phosphate = glycerone phosphate. P0A861 P0A861 5.3.1.1 Triose-phosphate isomerase. Phosphotriose isomerase. Triose phosphoisomerase. Triosephosphate isomerase. Triosephosphate mutase. D-glyceraldehyde 3-phosphate = glycerone phosphate. P0A862 P0A862 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0A867 P0A867 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. P0A870 P0A870 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. P0A871 P0A871 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. P0A872 P0A872 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. P0A877 P0A877 4.2.1.20 Tryptophan synthase. Indoleglycerol phosphate aldolase. L-tryptophan synthetase. Tryptophan desmolase. Tryptophan synthetase. L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. Pyridoxal 5'-phosphate. -!- The alpha-subunit catalyzes the conversion of 1-C-(indol-3- yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8). -!- The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. -!- In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24. -!- In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). -!- That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex. P0A889 P0A889 2.1.1.163 Demethylmenaquinone methyltransferase. 2-demethylmenaquinone methyltransferase. 2-heptaprenyl-1,4-naphthoquinone methyltransferase. Demethylmenaquinone C-methylase. A demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + S-adenosyl-L-homocysteine. -!- The enzyme catalyzes the last step in menaquinone biosynthesis. -!- It is able to accept substrates with varying polyprenyl side chain length (the chain length is determined by polyprenyl diphosphate synthase). -!- The enzyme from Escherichia coli also catalyzes the conversion of 2-methoxy-6-octaprenyl-1,4-benzoquinone to 5-methoxy-2-methyl-3- octaprenyl-1,4-benzoquinone during the biosynthesis of ubiquinone. -!- The enzyme probably acts on menaquinol rather than menaquinone. P0A889 P0A889 2.1.1.201 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase. S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4- benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans- polyprenyl-1,4-benzoquinol. -!- This enzyme is involved in ubiquinone biosynthesis. -!- Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. -!- However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. -!- For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant. -!- The bifunctional enzyme from E.coli also catalyzes the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163). P0A8A6 P0A8A6 2.7.4.28 ([Pyruvate, water dikinase] phosphate) phosphotransferase. PSRP. [Pyruvate, water dikinase] phosphate + phosphate = [pyruvate, water dikinase] + diphosphate. -!- The enzyme from the bacterium Escherichia coli is bifunctional and catalyzes both the phosphorylation and dephosphorylation of pyruvate, water dikinase (EC 2.7.9.2), cf. EC 2.7.11.33. -!- Formerly EC 2.7.4.n2. P0A8A6 P0A8A6 2.7.11.33 [Pyruvate, water dikinase] kinase. PEPS kinase. PSRP. ADP + [pyruvate, water dikinase] = AMP + [pyruvate, water dikinase] phosphate. -!- The enzyme from the bacterium Escherichia coli is bifunctional and catalyzes both the phosphorylation and dephosphorylation of EC 2.7.9.2; cf. EC 2.7.4.28. -!- The enzyme is specific for a reaction intermediate form of EC 2.7.9.2, where it phosphorylates an active site histidine. -!- It has no activity toward EC 2.7.9.1, (cf. EC 2.7.11.32). -!- Formerly EC 2.7.11.n2. P0A8F2 P0A8F2 2.4.2.9 Uracil phosphoribosyltransferase. UMP diphosphorylase. UMP pyrophosphorylase. UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. P0A8F3 P0A8F3 2.4.2.9 Uracil phosphoribosyltransferase. UMP diphosphorylase. UMP pyrophosphorylase. UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. P0A8F4 P0A8F4 2.7.1.48 Uridine kinase. Uridine monophosphokinase. ATP + uridine = ADP + UMP. -!- Cytidine can act as acceptor. -!- GTP and ITP can act as donors. P0A8F7 P0A8F7 2.7.1.48 Uridine kinase. Uridine monophosphokinase. ATP + uridine = ADP + UMP. -!- Cytidine can act as acceptor. -!- GTP and ITP can act as donors. P0A8G6 P0A8G6 1.6.5.2 NAD(P)H dehydrogenase (quinone). Azoreductase. Dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone). Diaphorase. DT-diaphorase. Flavoprotein NAD(P)H-quinone reductase. Menadione oxidoreductase. Menadione reductase. NAD(P)H dehydrogenase. NAD(P)H menadione reductase. NAD(P)H(2) dehydrogenase (quinone). NAD(P)H-quinone dehydrogenase. NAD(P)H-quinone oxidoreductase. NAD(P)H: menadione oxidoreductase. NAD(P)H:(quinone-acceptor)oxidoreductase. NADH-menadione reductase. Naphthoquinone reductase. p-benzoquinone reductase. Phylloquinone reductase. Quinone reductase. Reduced NAD(P)H dehydrogenase. Reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase. Viologen accepting pyridine nucleotide oxidoreductase. Vitamin K reductase. Vitamin-K reductase. NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone. FAD. -!- The enzyme catalyzes a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone. -!- The animal, but not the plant, form of the enzyme is inhibited by dicoumarol. -!- Formerly EC 1.6.99.2. P0A8G8 P0A8G8 1.6.5.2 NAD(P)H dehydrogenase (quinone). Azoreductase. Dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone). Diaphorase. DT-diaphorase. Flavoprotein NAD(P)H-quinone reductase. Menadione oxidoreductase. Menadione reductase. NAD(P)H dehydrogenase. NAD(P)H menadione reductase. NAD(P)H(2) dehydrogenase (quinone). NAD(P)H-quinone dehydrogenase. NAD(P)H-quinone oxidoreductase. NAD(P)H: menadione oxidoreductase. NAD(P)H:(quinone-acceptor)oxidoreductase. NADH-menadione reductase. Naphthoquinone reductase. p-benzoquinone reductase. Phylloquinone reductase. Quinone reductase. Reduced NAD(P)H dehydrogenase. Reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase. Viologen accepting pyridine nucleotide oxidoreductase. Vitamin K reductase. Vitamin-K reductase. NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone. FAD. -!- The enzyme catalyzes a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone. -!- The animal, but not the plant, form of the enzyme is inhibited by dicoumarol. -!- Formerly EC 1.6.99.2. P0A8L3 P0A8L3 6.1.1.11 Serine--tRNA ligase. Serine translase. SerRS. Seryl-transfer ribonucleate synthetase. Seryl-transfer ribonucleic acid synthetase. Seryl-transfer RNA synthetase. Seryl-tRNA synthetase. (1) ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). (2) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). -!- This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1. P0A8M0 P0A8M0 6.1.1.22 Asparagine--tRNA ligase. Asparagine translase. Asparaginyl-tRNA synthetase. ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl- tRNA(Asn). P0A8M3 P0A8M3 6.1.1.3 Threonine--tRNA ligase. Threonine translase. Threonyl-tRNA synthetase. ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). P0A8M5 P0A8M5 6.1.1.3 Threonine--tRNA ligase. Threonine translase. Threonyl-tRNA synthetase. ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). P0A8N3 P0A8N3 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). P0A8N5 P0A8N5 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). P0A8T7 P0A8T7 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A8T8 P0A8T8 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A8T9 P0A8T9 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A8V2 P0A8V2 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A8V4 P0A8V4 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A8V5 P0A8V5 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P0A8Y3 P0A8Y3 3.1.3.10 Glucose-1-phosphatase. Alpha-D-glucose 1-phosphate + H(2)O = D-glucose + phosphate. -!- Also acts, more slowly, on alpha-D-galactose 1-phosphate. P0A8Y5 P0A8Y5 3.1.3.23 Sugar-phosphatase. Sugar phosphate + H(2)O = sugar + phosphate. -!- Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate. P0A8Y7 P0A8Y7 3.1.3.23 Sugar-phosphatase. Sugar phosphate + H(2)O = sugar + phosphate. -!- Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate. P0A949 P0A949 2.3.1.267 [Ribosomal protein S5]-alanine N-acetyltransferase. Acetyl-CoA + an N-terminal L-alanyl-[S5 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S5 protein of 30S ribosome]. -!- The enzyme, characterized from bacteria, is specific for protein S5, a component of the 30S ribosomal subunit. -!- It also plays a role in maturation of the 30S ribosomal subunit. -!- Cf. EC 2.3.1.266. -!- Formerly EC 2.3.1.128. P0A953 P0A953 2.3.1.41 Beta-ketoacyl-[acyl-carrier-protein] synthase I. 3-ketoacyl-acyl carrier protein synthase. 3-oxoacyl-[acyl-carrier-protein] synthase. Acyl-malonyl acyl carrier protein-condensing enzyme. Acyl-malonyl(acyl-carrier-protein)-condensing enzyme. Beta-ketoacyl acyl carrier protein synthase. Beta-ketoacyl synthetase. Beta-ketoacyl-[acyl carrier protein] synthase. Beta-ketoacyl-ACP synthase I. Beta-ketoacyl-ACP synthetase. Beta-ketoacyl-acyl carrier protein synthetase. Beta-ketoacylsynthase. Condensing enzyme. Fatty acid condensing enzyme. KAS I. Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. -!- Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. -!- Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature. P0A955 P0A955 4.1.2.14 2-dehydro-3-deoxy-phosphogluconate aldolase. 2-dehydro-3-deoxy-D-gluconate-6-phosphate D-glyceraldehyde-3-phosphate- lyase. 2-keto-3-deoxy-6-phosphogluconate aldolase. KDPG-aldolase. Phospho-2-dehydro-3-deoxygluconate aldolase. Phospho-2-keto-3-deoxygluconate aldolase. 2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate. -!- The enzyme shows no activity with 2-dehydro-3-deoxy-6-phosphate-D- galactonate (cf. EC 4.1.2.55). -!- Also acts on 2-oxobutanoate. P0A955 P0A955 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase. 2-keto-4-hydroxyglutarate aldolase. 2-oxo-4-hydroxyglutarate aldolase. 4-hydroxy-2-oxoglutarate glyoxylate-lyase. KHG-aldolase. KHGA. 4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. -!- The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. -!- Formerly EC 4.1.2.1 and EC 4.1.2.31. P0A961 P0A961 2.6.1.2 Alanine transaminase. Alanine aminotransferase. Glutamic--alanine transaminase. Glutamic--pyruvic transaminase. L-alanine + 2-oxoglutarate = pyruvate + L-glutamate. Pyridoxal 5'-phosphate. -!- 2-aminobutanoate acts slowly instead of alanine. P0A991 P0A991 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P0A993 P0A993 3.1.3.11 Fructose-bisphosphatase. Fructose 1,6-bisphosphatase. Hexose diphosphatase. D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. -!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. P0A995 P0A995 3.1.3.11 Fructose-bisphosphatase. Fructose 1,6-bisphosphatase. Hexose diphosphatase. D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. -!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. P0A998 P0A998 1.16.3.2 Bacterial non-heme ferritin. 4 Fe(2+) + O(2) + 6 H(2)O = 4 (FeO(OH)) + 8 H(+). -!- Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life. -!- They are formed from two subunits that co-assemble in various ratios to form a spherical protein shell. -!- Thousands of mineralized iron atoms are stored within the core of the structure. -!- The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction. P0A9B2 P0A9B2 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. P0A9B4 P0A9B4 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. P0A9B5 P0A9B5 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. P0A9C0 P0A9C0 1.1.5.3 Glycerol-3-phosphate dehydrogenase. FAD-dependent glycerol-3-phosphate dehydrogenase. Flavin-linked glycerol-3-phosphate dehydrogenase. Glycerol-3-phosphate CoQ reductase. Glycerophosphate dehydrogenase. L-glycerophosphate dehydrogenase. sn-glycerol-3-phosphate dehydrogenase. sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. Flavin. -!- An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. -!- In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane. -!- In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain. -!- This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix. -!- Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9). -!- The enzyme is activated by calcium. -!- Formerly EC 1.1.2.1 and EC 1.1.99.5. P0A9C3 P0A9C3 5.1.3.3 Aldose 1-epimerase. Aldose mutarotase. Mutarotase. Alpha-D-glucose = beta-D-glucose. -!- Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. -!- This enzyme catalyzes the first step in galactose metabolism by converting beta-D-galactose into alpha-D-galactose, which is the substrate for EC 2.7.1.6. P0A9C5 P0A9C5 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. P0A9C7 P0A9C7 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. P0A9C8 P0A9C8 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. P0A9D2 P0A9D2 2.5.1.18 Glutathione transferase. Glutathione S-alkyltransferase. Glutathione S-aralkyltransferase. Glutathione S-aryltransferase. S-(hydroxyalkyl)glutathione lyase. RX + glutathione = HX + R-S-glutathione. -!- A group of enzymes of broad specificity. -!- R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. -!- Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. -!- Formerly EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7. P0A9D8 P0A9D8 2.3.1.117 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. Tetrahydrodipicolinate N-succinyltransferase. Tetrahydrodipicolinate succinylase. Tetrahydrodipicolinate succinyltransferase. Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. -!- Involved in the biosynthesis of lysine in bacteria, cyanobacteria and higher plants. -!- Earlier erroneously called 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase. P0A9G6 P0A9G6 4.1.3.1 Isocitrate lyase. ICL. Isocitrase. Isocitratase. Isocitrate glyoxylate-lyase. Isocitritase. Isocitrate = succinate + glyoxylate. -!- The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3- tricarboxylate. P0A9H1 P0A9H1 3.2.2.28 Double-stranded uracil-DNA glycosylase. DsUDG. Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil. -!- No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N(4)-ethenocytosine residue, significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing Escherichia coli. -!- Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. -!- Uracil-DNA glycosylase (EC 3.2.2.27) and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolyzing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalyzing the removal of mis-incorporated uracil from DNA. P0A9J6 P0A9J6 2.7.1.15 Ribokinase. ATP + D-ribose = ADP + D-ribose 5-phosphate. -!- 2-deoxy-D-ribose can also act as acceptor. P0A9J8 P0A9J8 4.2.1.51 Prephenate dehydratase. Prephenate = phenylpyruvate + H(2)O + CO(2). -!- This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate. P0A9J8 P0A9J8 5.4.99.5 Chorismate mutase. Hydroxyphenylpyruvate synthase. Chorismate = prephenate. P0A9L3 P0A9L3 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. P0A9M0 P0A9M0 3.4.21.53 Endopeptidase La. ATP-dependent protease La. ATP-dependent serine proteinase. Hydrolysis of proteins in presence of ATP. -!- ATP hydrolysis is linked with peptide bond hydrolysis. -!- Vanadate inhibits both reactions. -!- A similar enzyme occurs in animal mitochondria. -!- Belongs to peptidase family S16. P0A9M2 P0A9M2 2.4.2.8 Hypoxanthine phosphoribosyltransferase. Guanine phosphoribosyltransferase. HGPRTase. Hypoxanthine-guanine phosphoribosyltransferase. IMP diphosphorylase. IMP pyrophosphorylase. Transphosphoribosidase. IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. -!- Guanine and 6-mercaptopurine can replace hypoxanthine. P0A9M5 P0A9M5 2.4.2.22 Xanthine phosphoribosyltransferase. Xan phosphoribosyltransferase. Xanthine-guanine phosphoribosyltransferase. Xanthosine 5'-phosphate pyrophosphorylase. Xanthylate pyrophosphorylase. Xanthylic pyrophosphorylase. XMP pyrophosphorylase. XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine. P0A9M6 P0A9M6 2.4.2.22 Xanthine phosphoribosyltransferase. Xan phosphoribosyltransferase. Xanthine-guanine phosphoribosyltransferase. Xanthosine 5'-phosphate pyrophosphorylase. Xanthylate pyrophosphorylase. Xanthylic pyrophosphorylase. XMP pyrophosphorylase. XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine. P0A9M8 P0A9M8 2.3.1.8 Phosphate acetyltransferase. Phosphoacylase. Phosphotransacetylase. Acetyl-CoA + phosphate = CoA + acetyl phosphate. -!- Also acts with other short-chain acyl-CoAs. P0A9M9 P0A9M9 2.3.1.8 Phosphate acetyltransferase. Phosphoacylase. Phosphotransacetylase. Acetyl-CoA + phosphate = CoA + acetyl phosphate. -!- Also acts with other short-chain acyl-CoAs. P0A9N7 P0A9N7 1.97.1.4 [Formate-C-acetyltransferase]-activating enzyme. [Pyruvate formate-lyase]-activating enzyme. Formate acetyltransferase activating enzyme. Formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L- methionine oxidoreductase (S-adenosyl-L-methionine cleaving). PFL activase. PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving). Pyruvate formate-lyase 1 activating enzyme. S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical. Iron-sulfur. -!- A single glycine residue in EC 2.3.1.54 is oxidized to the corresponding radical by transfer of H from its CH(2) to AdoMet with concomitant cleavage of the latter. -!- The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5'-yl radical, which then abstracts a hydrogen radical from the glycine residue. P0A9P0 P0A9P0 1.8.1.4 Dihydrolipoyl dehydrogenase. Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. FAD. -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3. P0A9P2 P0A9P2 1.8.1.4 Dihydrolipoyl dehydrogenase. Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. FAD. -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3. P0A9P3 P0A9P3 1.8.1.4 Dihydrolipoyl dehydrogenase. Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. FAD. -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3. P0A9Q7 P0A9Q7 1.1.1.1 Alcohol dehydrogenase. Aldehyde reductase. (1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH. Zn(2+) or Fe cation. -!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. P0A9Q7 P0A9Q7 1.2.1.10 Acetaldehyde dehydrogenase (acetylating). Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating). Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH. -!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87. -!- Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. -!- NADP(+) can replace NAD(+) but the rate of reaction is much slower. P0A9Q8 P0A9Q8 1.1.1.1 Alcohol dehydrogenase. Aldehyde reductase. (1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH. Zn(2+) or Fe cation. -!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. P0A9Q8 P0A9Q8 1.2.1.10 Acetaldehyde dehydrogenase (acetylating). Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating). Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH. -!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87. -!- Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. -!- NADP(+) can replace NAD(+) but the rate of reaction is much slower. P0A9Q9 P0A9Q9 1.2.1.11 Aspartate-semialdehyde dehydrogenase. ASA dehydrogenase. Aspartic semialdehyde dehydrogenase. L-aspartate-beta-semialdehyde dehydrogenase. L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH. P0A9S3 P0A9S3 1.1.1.251 Galactitol-1-phosphate 5-dehydrogenase. Galactitol 1-phosphate + NAD(+) = D-tagatose 6-phosphate + NADH. Zn(2+). -!- The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway. P0A9T0 P0A9T0 1.1.1.95 Phosphoglycerate dehydrogenase. 3-phosphoglycerate dehydrogenase. 3-phosphoglyceric acid dehydrogenase. 3PHP reductase. Alpha-KG reductase. Alpha-phosphoglycerate dehydrogenase. D-3-phosphoglycerate dehydrogenase. Glycerate 3-phosphate dehydrogenase. Glycerate-1,3-phosphate dehydrogenase. PGDH. Phosphoglycerate oxidoreductase. Phosphoglyceric acid dehydrogenase. 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. -!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399. P0A9T0 P0A9T0 1.1.1.399 2-oxoglutarate reductase. (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. -!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95. P0A9T3 P0A9T3 1.1.1.95 Phosphoglycerate dehydrogenase. 3-phosphoglycerate dehydrogenase. 3-phosphoglyceric acid dehydrogenase. 3PHP reductase. Alpha-KG reductase. Alpha-phosphoglycerate dehydrogenase. D-3-phosphoglycerate dehydrogenase. Glycerate 3-phosphate dehydrogenase. Glycerate-1,3-phosphate dehydrogenase. PGDH. Phosphoglycerate oxidoreductase. Phosphoglyceric acid dehydrogenase. 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. -!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399. P0A9T3 P0A9T3 1.1.1.399 2-oxoglutarate reductase. (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. -!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95. P0AAB6 P0AAB6 2.7.7.9 UTP--glucose-1-phosphate uridylyltransferase. Glucose-1-phosphate uridylyltransferase. UDP-glucose diphosphorylase. UDP-glucose pyrophosphorylase. UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose. P0AAG8 P0AAG8 3.6.3.17 Monosaccharide-transporting ATPase. ATP + H(2)O + monosaccharide(Out) = ADP + phosphate + monosaccharide(In). -!- Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside. P0AAG9 P0AAG9 3.6.3.17 Monosaccharide-transporting ATPase. ATP + H(2)O + monosaccharide(Out) = ADP + phosphate + monosaccharide(In). -!- Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside. P0AAI8 P0AAI8 2.3.1.179 Beta-ketoacyl-[acyl-carrier-protein] synthase II. 3-oxoacyl-acyl carrier protein synthase I. Beta-ketoacyl-ACP synthase II. KAS II. KASII. (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier- protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. -!- Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. -!- While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme. -!- The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. -!- Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures. P0AAI9 P0AAI9 2.3.1.39 [Acyl-carrier-protein] S-malonyltransferase. Acyl carrier protein malonyltransferase. Malonyl coenzyme A-acyl carrier protein transacylase. Malonyl transacylase. Malonyl transferase. Malonyl-CoA-acyl carrier protein transacylase. Malonyl-CoA/dephospho-CoA acyltransferase. MCAT. Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein]. -!- Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria. -!- Also provides the malonyl groups for polyketide biosynthesis. -!- The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. -!- In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate. -!- This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89. -!- Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase. -!- In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates. -!- The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group. P0AB69 P0AB69 7.1.1.1 Proton-translocating NAD(P)(+) transhydrogenase. NADPH + NAD(+) + H(+)(Side 1) = NADP(+) + H(+)(Side 2) + NADH. -!- The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. -!- In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. -!- Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme. -!- Formerly EC 1.6.1.5. P0AB70 P0AB70 7.1.1.1 Proton-translocating NAD(P)(+) transhydrogenase. NADPH + NAD(+) + H(+)(Side 1) = NADP(+) + H(+)(Side 2) + NADH. -!- The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. -!- In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. -!- Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme. -!- Formerly EC 1.6.1.5. P0AB71 P0AB71 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P0AB72 P0AB72 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P0AB73 P0AB73 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P0AB79 P0AB79 2.3.1.29 Glycine C-acetyltransferase. 2-amino-3-ketobutyrate coenzyme A ligase. Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate. Pyridoxal 5'-phosphate. -!- Acts in concert with EC 1.1.1.103 in the degradation of threonine to form glycine. -!- This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex. P0AB80 P0AB80 2.6.1.42 Branched-chain-amino-acid transaminase. Branched-chain amino acid aminotransferase. Transaminase B. L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. Pyridoxal 5'-phosphate. -!- Also acts on L-isoleucine and L-valine. -!- Different from EC 2.6.1.66. P0AB88 P0AB88 4.1.2.17 L-fuculose-phosphate aldolase. Fuculose aldolase. L-fuculose 1-phosphate aldolase. L-fuculose-1-phosphate lactaldehyde-lyase. L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. P0AB89 P0AB89 4.3.2.2 Adenylosuccinate lyase. Adenylosuccinase. Succino AMP-lyase. (1) N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (2) (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide. -!- Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5- aminoimidazole. P0AB92 P0AB92 2.5.1.54 3-deoxy-7-phosphoheptulonate synthase. 2-dehydro-3-deoxy-phosphoheptonate aldolase. 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). D-erythrose-4-phosphate-lyase. D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating). DAH7-P synthase. DAHP synthase. Deoxy-D-arabino-heptulosonate-7-phosphate synthetase. DHAP synthase. DS-Co. DS-Mn. KDPH synthase. KDPH synthetase. Phospho-2-dehydro-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptanoate aldolase. Phospho-2-keto-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptonic aldolase. Phospho-2-oxo-3-deoxyheptonate aldolase. Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D- arabino-hept-2-ulosonate 7-phosphate + phosphate. -!- Formerly EC 4.1.2.15. P0ABB0 P0ABB0 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P0ABB2 P0ABB2 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P0ABB3 P0ABB3 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P0ABB4 P0ABB4 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P0ABB6 P0ABB6 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P0ABB7 P0ABB7 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P0ABB8 P0ABB8 7.2.2.14 P-type Mg(2+) transporter. Magnesium-translocating P-type ATPase. Mg(2+)-importing ATPase. Mg(2+)-transporting ATPase. Mg(2+)-transporting P-type ATPase. ATP + H(2)O + Mg(2+)(Side 1) = ADP + phosphate + Mg(2+)(Side 2). Mg(2+). -!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- A bacterial enzyme that imports Mg(2+) with, rather than against, the Mg(2+) electrochemical gradient. -!- The enzyme is also involved in Ni(2+) import. -!- Formerly EC 3.6.3.2. P0ABD5 P0ABD5 2.1.3.15 Acetyl-CoA carboxytransferase. [Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl- CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl- CoA. -!- The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. -!- In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2). -!- Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3). P0ABD7 P0ABD7 2.1.3.15 Acetyl-CoA carboxytransferase. [Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl- CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl- CoA. -!- The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. -!- In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2). -!- Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3). P0ABF6 P0ABF6 3.5.4.5 Cytidine deaminase. (Deoxy)cytidine deaminase. Cytidine aminohydrolase. Cytosine nucleoside deaminase. (1) Cytidine + H(2)O = uridine + NH(3). (2) 2'-deoxycytidine + H(2)O = 2'-deoxyuridine + NH(3). Zn(2+). -!- Catalyzes the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. -!- The enzyme, which is widely distributed among organisms, is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. -!- Formerly EC 3.5.4.14. P0ABH7 P0ABH7 2.3.3.16 Citrate synthase (unknown stereospecificity). Citrate condensing enzyme. Citrate synthetase. Citric synthase. Citric-condensing enzyme. Citrogenase. CoA-acetylating citrate oxaloacetate-lyase. Condensing enzyme. Oxalacetic transacetase. Oxaloacetate transacetase. Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. -!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3). P0ABH8 P0ABH8 2.3.3.16 Citrate synthase (unknown stereospecificity). Citrate condensing enzyme. Citrate synthetase. Citric synthase. Citric-condensing enzyme. Citrogenase. CoA-acetylating citrate oxaloacetate-lyase. Condensing enzyme. Oxalacetic transacetase. Oxaloacetate transacetase. Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. -!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3). P0ABJ9 P0ABJ9 7.1.1.7 Ubiquinol oxidase (electrogenic, proton-motive force generating). Cytochrome bd-I oxidase. 2 ubiquinol + O(2)(Side 2) + 4 H(+)(Side 2) = 2 ubiquinone + 2 H(2)O(Side 2) + 4 H(+)(Side 1). -!- This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. -!- The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. -!- The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. -!- Cf. EC 7.1.1.3. -!- Formerly EC 1.10.3.14. P0ABK1 P0ABK1 7.1.1.7 Ubiquinol oxidase (electrogenic, proton-motive force generating). Cytochrome bd-I oxidase. 2 ubiquinol + O(2)(Side 2) + 4 H(+)(Side 2) = 2 ubiquinone + 2 H(2)O(Side 2) + 4 H(+)(Side 1). -!- This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. -!- The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. -!- The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. -!- Cf. EC 7.1.1.3. -!- Formerly EC 1.10.3.14. P0ABK4 P0ABK4 7.1.1.7 Ubiquinol oxidase (electrogenic, proton-motive force generating). Cytochrome bd-I oxidase. 2 ubiquinol + O(2)(Side 2) + 4 H(+)(Side 2) = 2 ubiquinone + 2 H(2)O(Side 2) + 4 H(+)(Side 1). -!- This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. -!- The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. -!- The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. -!- Cf. EC 7.1.1.3. -!- Formerly EC 1.10.3.14. P0ABK5 P0ABK5 2.5.1.47 Cysteine synthase. Acetylserine sulfhydrylase. Cysteine synthetase. O(3)-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide). O-acetyl-L-serine sulfhydrylase. O-acetyl-L-serine sulfohydrolase. O-acetylserine (thiol)-lyase. O-acetylserine (thiol)-lyase A. O-acetylserine sulfhydrylase. OAS sulfhydrylase. O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate. Pyridoxal 5'-phosphate. -!- Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. -!- Not identical with EC 2.5.1.51, EC 2.5.1.52 and EC 2.5.1.53. -!- Formerly EC 4.2.99.8. P0ABK5 P0ABK5 4.5.1.5 S-carboxymethylcysteine synthase. 3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride. Pyridoxal 5'-phosphate. P0ABP8 P0ABP8 2.4.2.1 Purine-nucleoside phosphorylase. Inosine phosphorylase. PNPase. (1) Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. (2) Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate. -!- Specificity not completely determined. -!- Can also catalyze ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5. P0ABQ4 P0ABQ4 1.5.1.3 Dihydrofolate reductase. Tetrahydrofolate dehydrogenase. 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. -!- The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate. -!- Formerly EC 1.5.1.4. P0ABT0 P0ABT0 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P0ABZ8 P0ABZ8 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. P0AC13 P0AC13 2.5.1.15 Dihydropteroate synthase. DHPS. Dihydropteroate diphosphorylase. Dihydropteroate pyrophosphorylase. 6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate. -!- The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). -!- The enzyme exists in varying types of multifunctional proteins in different organisms. -!- The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25. P0AC15 P0AC15 2.5.1.15 Dihydropteroate synthase. DHPS. Dihydropteroate diphosphorylase. Dihydropteroate pyrophosphorylase. 6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate. -!- The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). -!- The enzyme exists in varying types of multifunctional proteins in different organisms. -!- The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25. P0AC33 P0AC33 4.2.1.2 Fumarate hydratase. Fumarase. (S)-malate = fumarate + H(2)O. P0AC33 P0AC33 5.3.2.2 Oxaloacetate tautomerase. Oxalacetic keto--enol isomerase. Oxaloacetate keto--enol tautomerase. Keto-oxaloacetate = enol-oxaloacetate. P0AC38 P0AC38 4.3.1.1 Aspartate ammonia-lyase. Aspartase. Fumaric aminase. L-aspartate = fumarate + NH(3). P0AC40 P0AC40 4.3.1.1 Aspartate ammonia-lyase. Aspartase. Fumaric aminase. L-aspartate = fumarate + NH(3). P0AC41 P0AC41 1.3.5.1 Succinate dehydrogenase (quinone). Succinate dehydrogenase (ubiquinone). Succinic dehydrogenase. Succinate + a quinone = fumarate + a quinol. FAD; Iron-sulfur. -!- The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. -!- It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). -!- In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. -!- Cf. EC 1.3.5.4. P0AC47 P0AC47 1.3.5.1 Succinate dehydrogenase (quinone). Succinate dehydrogenase (ubiquinone). Succinic dehydrogenase. Succinate + a quinone = fumarate + a quinol. FAD; Iron-sulfur. -!- The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. -!- It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). -!- In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. -!- Cf. EC 1.3.5.4. P0AC50 P0AC50 1.3.5.1 Succinate dehydrogenase (quinone). Succinate dehydrogenase (ubiquinone). Succinic dehydrogenase. Succinate + a quinone = fumarate + a quinol. FAD; Iron-sulfur. -!- The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. -!- It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). -!- In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. -!- Cf. EC 1.3.5.4. P0AC81 P0AC81 4.4.1.5 Lactoylglutathione lyase. (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing). Aldoketomutase. Glyoxalase I. Ketone-aldehyde mutase. Methylglyoxalase. (R)-S-lactoylglutathione = glutathione + methylglyoxal. -!- Also acts on 3-phosphoglycerol-glutathione. P0AC87 P0AC87 2.4.1.1 Glycogen phosphorylase. Amylophosphorylase. Muscle phosphorylase a and b. Polyphosphorylase. ((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. -!- This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. -!- Some of these enzymes catalyze the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. -!- The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. -!- The description (accepted name) of the enzyme should be modified for each specific instance by substituting 'glycogen' with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc. P0AC90 P0AC90 4.2.1.47 GDP-mannose 4,6-dehydratase. GDP-D-mannose 4,6-dehydratase. GDP-D-mannose dehydratase. Guanosine 5'-diphosphate-D-mannose oxidoreductase. Guanosine diphosphomannose 4,6-dehydratase. Guanosine diphosphomannose oxidoreductase. GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H(2)O. NAD(+). -!- Forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-alpha-L-fucose. -!- In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalyzing the above reaction as well as the reaction catalyzed by EC 1.1.1.281. P0AC91 P0AC91 4.2.1.47 GDP-mannose 4,6-dehydratase. GDP-D-mannose 4,6-dehydratase. GDP-D-mannose dehydratase. Guanosine 5'-diphosphate-D-mannose oxidoreductase. Guanosine diphosphomannose 4,6-dehydratase. Guanosine diphosphomannose oxidoreductase. GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H(2)O. NAD(+). -!- Forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-alpha-L-fucose. -!- In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalyzing the above reaction as well as the reaction catalyzed by EC 1.1.1.281. P0ACB3 P0ACB3 4.2.1.24 Porphobilinogen synthase. Aminolevulinate dehydratase. Delta-aminolevulinic acid dehydratase. 2 5-aminolevulinate = porphobilinogen + 2 H(2)O. Zn(2+). -!- The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. -!- The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. -!- In humans, the enzyme is a primary target for the environmental toxin Pb. -!- The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation. P0ACB4 P0ACB4 1.3.5.3 Protoporphyrinogen IX dehydrogenase (menaquinone). Protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol. -!- This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments. P0ACC2 P0ACC2 2.1.1.297 Peptide chain release factor N(5)-glutamine methyltransferase. N(5)-glutamine MTase. N(5)-glutamine S-adenosyl-L-methionine dependent methyltransferase. S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L- glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine. -!- Modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity. -!- Formerly EC 2.1.1.n16. P0ACD8 P0ACD8 1.12.99.6 Hydrogenase (acceptor). H(2) producing hydrogenase. Hydrogen-lyase. Hydrogenlyase. Uptake hydrogenase. H(2) + A = AH(2). Iron-sulfur; Ni(2+). -!- Uses molecular hydrogen for the reduction of a variety of substances. P0ACE2 P0ACE2 1.12.99.6 Hydrogenase (acceptor). H(2) producing hydrogenase. Hydrogen-lyase. Hydrogenlyase. Uptake hydrogenase. H(2) + A = AH(2). Iron-sulfur; Ni(2+). -!- Uses molecular hydrogen for the reduction of a variety of substances. P0ACZ3 P0ACZ3 3.1.3.48 Protein-tyrosine-phosphatase. Phosphotyrosine phosphatase. PTPase. Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. -!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2. P0AD61 P0AD61 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). P0AD62 P0AD62 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). P0ADG7 P0ADG7 1.1.1.205 IMP dehydrogenase. IMP oxidoreductase. Inosinate dehydrogenase. Inosine 5'-monophosphate dehydrogenase. Inosine monophosphate oxidoreductase. Inosinic acid dehydrogenase. Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH. -!- The enzyme acts on the hydroxy group of the hydrated derivative of the substrate. -!- Formerly EC 1.2.1.14. P0ADG8 P0ADG8 1.1.1.205 IMP dehydrogenase. IMP oxidoreductase. Inosinate dehydrogenase. Inosine 5'-monophosphate dehydrogenase. Inosine monophosphate oxidoreductase. Inosinic acid dehydrogenase. Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH. -!- The enzyme acts on the hydroxy group of the hydrated derivative of the substrate. -!- Formerly EC 1.2.1.14. P0ADI4 P0ADI4 3.3.2.1 Isochorismatase. 2,3-dihydro-2,3-dihydroxybenzoate synthase. Isochorismate + H(2)O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate. P0ADI4 P0ADI4 6.3.2.14 Enterobactin synthase. 2,3-dihydroxybenzoate--serine ligase. N-(2,3-dihydroxybenzoyl)-serine synthetase. 6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate. -!- This enzyme complex catalyzes the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. -!- In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyzes the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyzes the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3- dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule). P0ADR7 P0ADR7 2.1.1.186 23S rRNA (cytidine(2498)-2'-O)-methyltransferase. S-adenosyl-L-methionine + cytidine(2498) in 23S rRNA = S-adenosyl-L- homocysteine + 2'-O-methylcytidine(2498) in 23S rRNA. P0AE08 P0AE08 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0AE10 P0AE10 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0AE11 P0AE11 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0AE12 P0AE12 3.2.2.4 AMP nucleosidase. AMP + H(2)O = D-ribose 5-phosphate + adenine. P0AE18 P0AE18 3.4.11.18 Methionyl aminopeptidase. Methionine aminopeptidase. Peptidase M. Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Cobalt cation. -!- This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. -!- The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). -!- Belongs to peptidase family M24A. P0AE20 P0AE20 3.4.11.18 Methionyl aminopeptidase. Methionine aminopeptidase. Peptidase M. Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Cobalt cation. -!- This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. -!- The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). -!- Belongs to peptidase family M24A. P0AE21 P0AE21 3.4.11.18 Methionyl aminopeptidase. Methionine aminopeptidase. Peptidase M. Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Cobalt cation. -!- This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. -!- The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). -!- Belongs to peptidase family M24A. P0AE52 P0AE52 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0AE54 P0AE54 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0AE55 P0AE55 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0AE82 P0AE82 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0AEB2 P0AEB2 3.4.16.4 Serine-type D-Ala-D-Ala carboxypeptidase. D-alanyl-D-alanine carboxypeptidase. DD-peptidase. DD-transpeptidase. Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. -!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13. P0AEB2 P0AEB2 3.5.2.6 Beta-lactamase. Cephalosporinase. Penicillinase. A beta-lactam + H(2)O = a substituted beta-amino acid. Zn(2+). -!- Zinc is only requires in class-B enzymes. -!- A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. -!- Formerly EC 3.5.2.8. P0AEC3 P0AEC3 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0AEI3 P0AEI3 2.8.4.3 tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase. 2-methylthio-N-6-isopentenyl adenosine synthase. tRNA-i6A37 methylthiotransferase. N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio- N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor. Iron-sulfur. -!- This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur. -!- The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes. -!- The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. -!- The identity of the electron donor is not known. P0AEJ4 P0AEJ4 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0AEK2 P0AEK2 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH. -!- Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates. P0AEK5 P0AEK5 1.3.1.9 Enoyl-[acyl-carrier-protein] reductase (NADH). Enoyl-ACP reductase. NADH-enoyl acyl carrier protein reductase. NADH-specific enoyl-ACP reductase. An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH. -!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons. P0AEP5 P0AEP5 2.7.7.9 UTP--glucose-1-phosphate uridylyltransferase. Glucose-1-phosphate uridylyltransferase. UDP-glucose diphosphorylase. UDP-glucose pyrophosphorylase. UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose. P0AES0 P0AES0 3.5.1.78 Glutathionylspermidine amidase. Glutathionylspermidine amidohydrolase (spermidine-forming). GSP amidase. Glutathionylspermidine + H(2)O = glutathione + spermidine. -!- Transforms glutathionylspermidine into glutathione and spermidine. -!- The enzyme from Escherichia coli is bifunctional and also catalyzes the reaction of EC 6.3.1.8, resulting in a net hydrolysis of ATP. P0AES0 P0AES0 6.3.1.8 Glutathionylspermidine synthase. Gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming). Glutathione:spermidine ligase (ADP-forming). Glutathionylspermidine synthetase. GSP synthetase. Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate. Mg(2+). -!- Involved in the synthesis of trypanothione in trypanosomatids. -!- The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 3.5.1.78 reaction, resulting in a net hydrolysis of ATP. P0AES5 P0AES5 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P0AES7 P0AES7 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P0AES8 P0AES8 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P0AET8 P0AET8 1.1.1.159 7-alpha-hydroxysteroid dehydrogenase. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD(+) = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH. -!- Catalyzes the oxidation of the 7-alpha-hydroxy group of bile acids and alcohols both in their free and conjugated forms. -!- The Bacteroides fragilis and Clostridium enzymes can also utilize NADP(+). P0AET9 P0AET9 1.1.1.159 7-alpha-hydroxysteroid dehydrogenase. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD(+) = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH. -!- Catalyzes the oxidation of the 7-alpha-hydroxy group of bile acids and alcohols both in their free and conjugated forms. -!- The Bacteroides fragilis and Clostridium enzymes can also utilize NADP(+). P0AF04 P0AF04 2.7.7.75 Molybdopterin adenylyltransferase. ATP + molybdopterin = diphosphate + adenylyl-molybdopterin. Mn(2+) or Mg(2+). -!- Catalyzes the activation of molybdopterin for molybdenum insertion. -!- In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1). -!- The reaction requires a divalent cation such as Mg(2+) or Mn(2+). -!- Catalyzes the activation of molybdopterin for molybdenum insertion. -!- In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes EC 2.10.1.1. -!- Formerly EC 2.7.7.n5. P0AF05 P0AF05 2.7.7.75 Molybdopterin adenylyltransferase. ATP + molybdopterin = diphosphate + adenylyl-molybdopterin. Mn(2+) or Mg(2+). -!- Catalyzes the activation of molybdopterin for molybdenum insertion. -!- In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1). -!- The reaction requires a divalent cation such as Mg(2+) or Mn(2+). -!- Catalyzes the activation of molybdopterin for molybdenum insertion. -!- In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes EC 2.10.1.1. -!- Formerly EC 2.7.7.n5. P0AF24 P0AF24 3.1.3.5 5'-nucleotidase. A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate. -!- Wide specificity for 5'-nucleotides. P0AF25 P0AF25 3.1.3.5 5'-nucleotidase. A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate. -!- Wide specificity for 5'-nucleotides. P0AF93 P0AF93 3.5.99.10 2-iminobutanoate/2-iminopropanoate deaminase. Enamine/imine deaminase. (1) 2-iminobutanoate + H(2)O = 2-oxobutanoate + NH(3). (2) 2-iminopropanoate + H(2)O = pyruvate + NH(3). -!- This enzyme, which has been found in all species and tissues examined, catalyzes the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19 and EC 4.3.1.17. -!- The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates. P0AFA3 P0AFA3 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0AFB5 P0AFB5 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0AFB6 P0AFB6 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0AFG5 P0AFG5 1.2.4.2 Oxoglutarate dehydrogenase (succinyl-transferring). 2-ketoglutarate dehydrogenase. 2-oxoglutarate dehydrogenase. 2-oxoglutarate: lipoate oxidoreductase. 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- succinylating). AKGDH. Alpha-ketoglutarate dehydrogenase. Alpha-ketoglutaric acid dehydrogenase. Alpha-ketoglutaric dehydrogenase. Alpha-oxoglutarate dehydrogenase. Ketoglutaric dehydrogenase. OGDC. Oxoglutarate decarboxylase. Oxoglutarate dehydrogenase. Oxoglutarate dehydrogenase (lipoamide). 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61. P0AFG6 P0AFG6 2.3.1.61 Dihydrolipoyllysine-residue succinyltransferase. Dihydrolipoamide S-succinyltransferase. Dihydrolipoamide succinyltransferase. Dihydrolipoic transsuccinylase. Dihydrolipolyl transsuccinylase. Dihydrolipoyl transsuccinylase. Lipoate succinyltransferase. Lipoic transsuccinylase. Lipoyl transsuccinylase. Succinyl-CoA:dihydrolipoamide S-succinyltransferase. Succinyl-CoA:dihydrolipoate S-succinyltransferase. Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine. -!- A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A. P0AFG8 P0AFG8 1.2.4.1 Pyruvate dehydrogenase (acetyl-transferring). MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase. Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. P0AFG9 P0AFG9 1.2.4.1 Pyruvate dehydrogenase (acetyl-transferring). MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase. Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. P0AFI8 P0AFI8 1.4.3.5 Pyridoxal 5'-phosphate synthase. PMP oxidase. Pyridoxamine 5'-phosphate oxidase. Pyridoxamine phosphate oxidase. Pyridoxamine-phosphate oxidase. Pyridoxine (pyridoxamine) 5'-phosphate oxidase. Pyridoxine (pyridoxamine)phosphate oxidase. (1) Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2). (2) Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-phosphate + H(2)O(2). FMN. -!- In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5. P0AFU9 P0AFU9 2.5.1.9 Riboflavin synthase. 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D- ribitylamino)-5-amino-2,6-dihydroxypyrimidine. P0AG07 P0AG07 5.1.3.1 Ribulose-phosphate 3-epimerase. D-ribulose phosphate-3-epimerase. D-ribulose-5-phosphate epimerase. D-xylulose-5-phosphate 3-epimerase. Erythrose-4-phosphate epimerase. Pentose-5-phosphate 3-epimerase. Phosphoribulose epimerase. Xylulose phosphate 3-epimerase. D-ribulose 5-phosphate = D-xylulose 5-phosphate. -!- Also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate. P0AG10 P0AG10 5.1.3.1 Ribulose-phosphate 3-epimerase. D-ribulose phosphate-3-epimerase. D-ribulose-5-phosphate epimerase. D-xylulose-5-phosphate 3-epimerase. Erythrose-4-phosphate epimerase. Pentose-5-phosphate 3-epimerase. Phosphoribulose epimerase. Xylulose phosphate 3-epimerase. D-ribulose 5-phosphate = D-xylulose 5-phosphate. -!- Also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate. P0AG23 P0AG23 2.7.6.5 GTP diphosphokinase. GTP pyrophosphokinase. Guanosine 3',5'-polyphosphate synthase. ppGpp synthetase I. Stringent factor. ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. -!- GDP can also act as acceptor. P0AG26 P0AG26 3.1.7.2 Guanosine-3',5'-bis(diphosphate) 3'-diphosphatase. (ppGpp)ase. Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase. Penta-phosphate guanosine-3'-diphosphohydrolase. Penta-phosphate guanosine-3'-pyrophosphohydrolase. Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate. P0AG40 P0AG40 2.7.1.26 Riboflavin kinase. Flavokinase. RFK. ATP + riboflavin = ADP + FMN. Mg(2+) or Zn(2+) or Mn(2+). -!- The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B(6), vitamin B12 and folates. -!- While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2. -!- In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP. P0AG40 P0AG40 2.7.7.2 FAD synthetase. FAD diphosphorylase. FAD pyrophosphorylase. FADS. Flavin adenine dinucleotide synthetase. FMN adenylyltransferase. ATP + FMN = diphosphate + FAD. Mg(2+). -!- Highly specific for ATP as phosphate donor. -!- The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates. -!- While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26. P0AGB0 P0AGB0 3.1.3.3 Phosphoserine phosphatase. O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate. P0AGD3 P0AGD3 1.15.1.1 Superoxide dismutase. 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Fe cation or Mn(2+) or (Zn(2+) and Cu cation). P0AGD6 P0AGD6 1.15.1.1 Superoxide dismutase. 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Fe cation or Mn(2+) or (Zn(2+) and Cu cation). P0AGE9 P0AGE9 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P0AGG4 P0AGG4 1.8.1.8 Protein-disulfide reductase. Disulfide reductase. Insulin-glutathione transhydrogenase. Protein disulfide reductase. Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H. -!- Formerly EC 1.6.4.4. P0AGJ9 P0AGJ9 6.1.1.1 Tyrosine--tRNA ligase. L-tyrosine-tRNA(Tyr) ligase (AMP-forming). Tyrosine translase. Tyrosine tRNA synthetase. Tyrosine-transfer ribonucleate synthetase. Tyrosine-transfer RNA ligase. Tyrosyl-transfer ribonucleate synthetase. Tyrosyl-transfer ribonucleic acid synthetase. Tyrosyl-transfer RNA synthetase. Tyrosyl-tRNA ligase. Tyrosyl-tRNA synthetase. ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). P0C037 P0C037 2.4.2.1 Purine-nucleoside phosphorylase. Inosine phosphorylase. PNPase. (1) Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. (2) Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate. -!- Specificity not completely determined. -!- Can also catalyze ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5. P0C037 P0C037 2.4.2.2 Pyrimidine-nucleoside phosphorylase. Py-NPase. (1) Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. (2) Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. (3) 2'-deoxyuridine + phosphate = uracil + 2-deoxy-alpha-D-ribose 1-phosphate. -!- Unlike EC 2.4.2.3 and EC 2.4.2.4, this enzyme can accept both the ribonucleoside uridine and the 2'-deoxyribonucleosides 2'-deoxyuridine and thymidine. -!- The reaction is reversible, and the enzyme does not distinguish between alpha-D-ribose 1-phosphate and 2-deoxy-alpha-D-ribose 1-phosphate in the synthetic direction. -!- Formerly EC 2.4.2.23. P0C037 P0C037 2.4.2.3 Uridine phosphorylase. Pyrimidine phosphorylase. UPase. UrdPase. Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. -!- The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. -!- The mammalian enzyme also accepts 2'-deoxyuridine. -!- Formerly EC 2.4.2.23. P0C037 P0C037 2.4.2.4 Thymidine phosphorylase. Pyrimidine phosphorylase. Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. -!- In some tissues also catalyzes deoxyribosyltransferase reactions of the type catalyzed by EC 2.4.2.6. -!- Formerly EC 2.4.2.23. P0C037 P0C037 2.4.2.15 Guanosine phosphorylase. Guanosine + phosphate = guanine + alpha-D-ribose 1-phosphate. -!- Also acts on deoxyguanosine. P0C039 P0C039 2.4.2.2 Pyrimidine-nucleoside phosphorylase. Py-NPase. (1) Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. (2) Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. (3) 2'-deoxyuridine + phosphate = uracil + 2-deoxy-alpha-D-ribose 1-phosphate. -!- Unlike EC 2.4.2.3 and EC 2.4.2.4, this enzyme can accept both the ribonucleoside uridine and the 2'-deoxyribonucleosides 2'-deoxyuridine and thymidine. -!- The reaction is reversible, and the enzyme does not distinguish between alpha-D-ribose 1-phosphate and 2-deoxy-alpha-D-ribose 1-phosphate in the synthetic direction. -!- Formerly EC 2.4.2.23. P0C039 P0C039 2.4.2.3 Uridine phosphorylase. Pyrimidine phosphorylase. UPase. UrdPase. Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. -!- The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. -!- The mammalian enzyme also accepts 2'-deoxyuridine. -!- Formerly EC 2.4.2.23. P0C039 P0C039 2.4.2.4 Thymidine phosphorylase. Pyrimidine phosphorylase. Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. -!- In some tissues also catalyzes deoxyribosyltransferase reactions of the type catalyzed by EC 2.4.2.6. -!- Formerly EC 2.4.2.23. P0C039 P0C039 2.4.2.15 Guanosine phosphorylase. Guanosine + phosphate = guanine + alpha-D-ribose 1-phosphate. -!- Also acts on deoxyguanosine. P0C061 P0C061 5.1.1.11 Phenylalanine racemase (ATP-hydrolyzing). ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine. P0C0F6 P0C0F6 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P0C0L2 P0C0L2 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P0C0R8 P0C0R8 2.1.1.166 23S rRNA (uridine(2552)-2'-O)-methyltransferase. FTSJ. Um(2552) 23S ribosomal RNA methyltransferase. Um2552 methyltransferase. S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = S-adenosyl-L- homocysteine + 2'-O-methyluridine(2552) in 23S rRNA. -!- The enzyme catalyzes the 2'-O-methylation of the universally conserved U2552 in the A loop of 23S rRNA. P0C0V0 P0C0V0 3.4.21.107 Peptidase Do. High temperature requirement protease A. HrtA heat shock protein. Protease Do. Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val. -!- This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli. -!- Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli. -!- The enzyme has weak peptidase activity with casein and other non- native substrates. -!- The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. -!- Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding. -!- They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding. -!- If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme. -!- Belongs to peptidase family S1B. P0C8J6 P0C8J6 4.1.2.40 Tagatose-bisphosphate aldolase. D-tagatose-1,6-bisphosphate aldolase. D-tagatose-1,6-bisphosphate triosephosphate lyase. Tagatose 1,6-diphosphate aldolase. D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. -!- Enzyme activity is stimulated by certain divalent cations. -!- Involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria. P0CI73 P0CI73 2.6.1.16 Glutamine--fructose-6-phosphate transaminase (isomerizing). D-fructose-6-phosphate amidotransferase. GlcN6P synthase. Glucosamine-6-phosphate isomerase (glutamine-forming). Glucosamine-6-phosphate synthase. Hexosephosphate aminotransferase. L-glutamine-D-fructose-6-phosphate amidotransferase. L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. -!- Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). -!- Formerly EC 5.3.1.19. P0CI75 P0CI75 6.3.4.15 Biotin--[biotin carboxyl-carrier protein] ligase. Acetyl-CoA carboxylase biotin holoenzyme synthetase. Biotin--[acetyl-CoA carboxylase] synthetase. Biotin--[acetyl-CoA-carboxylase] ligase. Biotin--protein ligase. ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine. -!- The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14. -!- The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15. -!- In some organisms the carrier protein is part of EC 6.4.1.2. P0CI80 P0CI80 5.3.1.5 Xylose isomerase. D-xylose ketoisomerase. D-xylopyranose = D-xylulose. Mg(2+). -!- The enzyme catalyzes the interconversion of aldose and ketose sugars with broad substrate specificity. -!- The enzyme binds the closed form of its sugar substrate (in the case of glucose, only the alpha anomer) and catalyzes ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. -!- Isomerization proceeds via a hydride-shift mechanism. P0DJF8 P0DJF8 2.4.2.28 S-methyl-5'-thioadenosine phosphorylase. 5'-deoxy-5'-methylthioadenosine phosphorylase. 5'-methylthioadenosine phosphorylase. MeSAdo phosphorylase. MeSAdo/Ado phosphorylase. Methylthioadenosine nucleoside phosphorylase. Methylthioadenosine phosphorylase. MTA phosphorylase. MTAPase. S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha- D-ribose 1-phosphate. -!- Also acts on 5'-deoxyadenosine and other analogs having 5'-deoxy groups. P0DM80 P0DM80 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P10908 P10908 3.1.4.46 Glycerophosphodiester phosphodiesterase. Glycerophosphoryl diester phosphodiesterase. A glycerophosphodiester + H(2)O = an alcohol + sn-glycerol 3-phosphate. -!- Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolyzed. P11044 P11044 2.1.1.45 Thymidylate synthase. 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. P11162 P11162 2.7.1.207 Protein-N(pi)-phosphohistidine--lactose phosphotransferase. Lactose PTS permease. [Protein]-N(pi)-phospho-L-histidine + lactose(Side 1) = [protein]-L- histidine + lactose 6'-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P11386 P11386 1.1.1.37 Malate dehydrogenase. Malic dehydrogenase. (S)-malate + NAD(+) = oxaloacetate + NADH. -!- Also oxidizes some other 2-hydroxydicarboxylic acids. P11447 P11447 4.3.2.1 Argininosuccinate lyase. Arginosuccinase. N-(L-argininosuccinate) arginine-lyase. Omega-N-(L-arginino)succinate arginine-lyase. 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. P11513 P11513 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P11875 P11875 6.1.1.19 Arginine--tRNA ligase. Arginine translase. Arginyl-tRNA synthetase. ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). P12042 P12042 6.3.5.3 Phosphoribosylformylglycinamidine synthase. FGAM synthase. FGAM synthetase. FGAR amidotransferase. FGARAT. Formylglycinamide ribotide amidotransferase. Phosphoribosylformylglycinamidine synthetase. ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine + L-glutamate. P12043 P12043 6.3.3.1 Phosphoribosylformylglycinamidine cyclo-ligase. AIR synthase. AIR synthetase. AIRS. Phosphoribosyl-aminoimidazole synthetase. Phosphoribosylaminoimidazole synthetase. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. P12046 P12046 6.3.2.6 Phosphoribosylaminoimidazolesuccinocarboxamide synthase. 4-((N-succinylamino)carbonyl)-5-aminoimidazole ribonucleotide synthetase. 4-(N-succinocarboxamide)-5-aminoimidazole synthetase. 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase. Phosphoribosylaminoimidazole-succinocarboxamide synthase. Phosphoribosylaminoimidazole-succinocarboxamide synthetase. Phosphoribosylaminoimidazolesuccinocarboxamide synthetase. SAICAR synthase. SAICAR synthetase. SAICARs. ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate. -!- Forms part of the purine biosynthesis pathway. P12048 P12048 2.1.2.3 Phosphoribosylaminoimidazolecarboxamide formyltransferase. 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4- imidazolecarboxamide formyltransferase. 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase. 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase. 5-amino-4-imidazolecarboxamide ribonucleotide transformylase. 5-amino-4-imidazolecarboxamide ribotide transformylase. AICAR formyltransferase. AICAR transformylase. Aminoimidazolecarboxamide ribonucleotide transformylase. 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide. P12048 P12048 3.5.4.10 IMP cyclohydrolase. IMP synthetase. Inosinicase. IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. P12425 P12425 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. P12758 P12758 2.4.2.3 Uridine phosphorylase. Pyrimidine phosphorylase. UPase. UrdPase. Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. -!- The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. -!- The mammalian enzyme also accepts 2'-deoxyuridine. -!- Formerly EC 2.4.2.23. P13029 P13029 1.11.1.21 Catalase peroxidase. (1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O. -!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. P13035 P13035 1.1.5.3 Glycerol-3-phosphate dehydrogenase. FAD-dependent glycerol-3-phosphate dehydrogenase. Flavin-linked glycerol-3-phosphate dehydrogenase. Glycerol-3-phosphate CoQ reductase. Glycerophosphate dehydrogenase. L-glycerophosphate dehydrogenase. sn-glycerol-3-phosphate dehydrogenase. sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. Flavin. -!- An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. -!- In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane. -!- In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain. -!- This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix. -!- Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9). -!- The enzyme is activated by calcium. -!- Formerly EC 1.1.2.1 and EC 1.1.99.5. P13243 P13243 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P13267 P13267 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P13484 P13484 2.4.1.52 Poly(glycerol-phosphate) alpha-glucosyltransferase. UDP glucose-poly(glycerol-phosphate) alpha-glucosyltransferase. n UDP-alpha-D-glucose + 4-O-(poly((2R)-glycerophospho)-(2R)- glycerophospho)-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D- glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O- (poly((2R)-2-alpha-D-glucosyl-1-glycerophospho)-(2R)-glycerophospho)-N- acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl- diphospho-ditrans,octacis-undecaprenol. -!- Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. -!- This enzyme, isolated from Bacillus subtilis 168, adds an alpha-D- glucose to the free OH groups of the glycerol units. -!- The enzyme has a strong preference for UDP-alpha-glucose as the sugar donor. -!- It has no activity with poly(ribitol phosphate). P13485 P13485 2.7.8.12 Teichoic acid poly(glycerol phosphate) polymerase. Poly(glycerol phosphate) polymerase. Tag polymerase. Teichoic acid glycerol transferase. Teichoic-acid synthase. n CDP-glycerol + 4-O-((2R)-glycerophospho)-N-acetyl-beta-D-mannosaminyl- (1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis- undecaprenol = n CMP + 4-O-(((2R)-glycerophospho)n-(2R)-glycerophospho)- N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl- diphospho-ditrans,octacis-undecaprenol. -!- Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. -!- This enzyme adds 30-50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44. -!- Cf. EC 2.7.8.45. P13714 P13714 1.1.1.27 L-lactate dehydrogenase. L-lactic acid dehydrogenase. L-lactic dehydrogenase. (S)-lactate + NAD(+) = pyruvate + NADH. -!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme. P13799 P13799 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P13981 P13981 3.5.3.6 Arginine deiminase. Arginine dihydrolase. L-arginine + H(2)O = L-citrulline + NH(3). -!- Also acts on canavanine. P14192 P14192 2.3.1.157 Glucosamine-1-phosphate N-acetyltransferase. Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate. -!- The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23. P14192 P14192 2.7.7.23 UDP-N-acetylglucosamine diphosphorylase. N-acetylglucosamine-1-phosphate uridyltransferase. UDP-N-acetylglucosamine pyrophosphorylase. UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine. -!- Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. -!- The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. -!- The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate. P14193 P14193 2.7.6.1 Ribose-phosphate diphosphokinase. Phosphoribosyl diphosphate synthetase. Phosphoribosyl pyrophosphate synthetase. Ribose-phosphate pyrophosphokinase. ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. -!- dATP can also act as donor. P14407 P14407 4.2.1.2 Fumarate hydratase. Fumarase. (S)-malate = fumarate + H(2)O. P14407 P14407 4.2.1.81 D(-)-tartrate dehydratase. (S,S)-tartrate = oxaloacetate + H(2)O. Fe cation. P14900 P14900 6.3.2.9 UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase. D-glutamate ligase. D-glutamate-adding enzyme. MurD synthetase. UDP-Mur-NAC-L-Ala:D-Glu ligase. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase. UDP-N-acetylmuramoylalanine--D-glutamate ligase. Uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase. ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate. -!- Involved in the synthesis of a cell-wall peptide in bacteria. P15042 P15042 6.5.1.2 DNA ligase (NAD(+)). DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (NAD(+)). Polydeoxyribonucleotide synthase (NAD+). Polynucleotide ligase (NAD(+)). Polynucleotide ligase (NAD+). NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide. -!- The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7. P15106 P15106 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. P15254 P15254 6.3.5.3 Phosphoribosylformylglycinamidine synthase. FGAM synthase. FGAM synthetase. FGAR amidotransferase. FGARAT. Formylglycinamide ribotide amidotransferase. Phosphoribosylformylglycinamidine synthetase. ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine + L-glutamate. P15288 P15288 3.4.13.18 Cytosol nonspecific dipeptidase. Cytosol non-specific dipeptidase. Glycyl-glycine dipeptidase. Glycyl-leucine dipeptidase. N(2)-beta-alanylarginine dipeptidase. Peptidase A. Pro-X dipeptidase. Prolinase. Prolyl dipeptidase. Prolylglycine dipeptidase. Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids. Zn(2+). -!- Broad specificity, varying somewhat with source species. -!- Activated and stabilized by dithiothreitol and manganese. -!- Inhibited by bestatin and leucine. -!- Belongs to peptidase family M20. -!- Formerly EC 3.4.3.1, EC 3.4.3.2, EC 3.4.3.3, EC 3.4.3.6, EC 3.4.13.1, EC 3.4.13.2, EC 3.4.13.3, EC 3.4.13.8, EC 3.4.13.11, EC 3.4.13.13 and EC 3.4.13.15. P16033 P16033 1.10.3.9 Photosystem II. 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2 plastoquinol. -!- Contains chlorophyll a, beta-carotene, pheophytin, plastoquinone, a Mn(4)Ca cluster, heme and non-heme iron. -!- Four successive photoreactions, resulting in a storage of four positive charges, are required to oxidize two water molecules to one oxygen molecule. P16263 P16263 2.3.1.61 Dihydrolipoyllysine-residue succinyltransferase. Dihydrolipoamide S-succinyltransferase. Dihydrolipoamide succinyltransferase. Dihydrolipoic transsuccinylase. Dihydrolipolyl transsuccinylase. Dihydrolipoyl transsuccinylase. Lipoate succinyltransferase. Lipoic transsuccinylase. Lipoyl transsuccinylase. Succinyl-CoA:dihydrolipoamide S-succinyltransferase. Succinyl-CoA:dihydrolipoate S-succinyltransferase. Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine. -!- A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A. P16575 P16575 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P16659 P16659 6.1.1.15 Proline--tRNA ligase. Proline translase. Prolyl-tRNA synthetase. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). P16676 P16676 7.3.2.3 ABC-type sulfate transporter. Sulfate ABC transporter. Sulfate-transporting ATPase. ATP + H(2)O + sulfate-[sulfate-binding protein](Side 1) = ADP + phosphate + sulfate(Side 2) + [sulfate-binding protein](Side 1). -!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- The enzyme from Escherichia coli can interact with either of two periplasmic binding proteins and mediates the high affinity uptake of sulfate and thiosulfate. -!- May also be involved in the uptake of selenite, selenate and possibly molybdate. -!- Does not undergo phosphorylation during the transport. -!- Formerly EC 3.6.3.25. P17443 P17443 2.4.1.227 Undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase. MurG transferase. UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl- undecaprenol N-acetylglucosamine transferase. Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase. UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D- Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma- D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. -!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. P17444 P17444 1.1.99.1 Choline dehydrogenase. Choline oxidase. Choline-cytochrome c reductase. Choline + acceptor = betaine aldehyde + reduced acceptor. Pyrroloquinoline quinone. -!- In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyze the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. -!- In plants, the first reaction is catalyzed by EC 1.14.15.7 whereas in animals and many bacteria, it is catalyzed by either EC 1.1.99.1 or EC 1.1.3.17. -!- The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria. P17444 P17444 1.2.1.8 Betaine-aldehyde dehydrogenase. BADH. Betaine aldehyde dehydrogenase. Betaine aldehyde oxidase. Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH. -!- In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. -!- This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. -!- In contrast, different enzymes are involved in the first reaction. -!- In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17. -!- In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157. P17922 P17922 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). P18009 P18009 2.3.2.27 RING-type E3 ubiquitin transferase. RING E3 ligase. Ubiquitin transferase RING E3. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine. -!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31. P18014 P18014 2.3.2.27 RING-type E3 ubiquitin transferase. RING E3 ligase. Ubiquitin transferase RING E3. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine. -!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31. P18158 P18158 1.1.5.3 Glycerol-3-phosphate dehydrogenase. FAD-dependent glycerol-3-phosphate dehydrogenase. Flavin-linked glycerol-3-phosphate dehydrogenase. Glycerol-3-phosphate CoQ reductase. Glycerophosphate dehydrogenase. L-glycerophosphate dehydrogenase. sn-glycerol-3-phosphate dehydrogenase. sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. Flavin. -!- An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. -!- In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane. -!- In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain. -!- This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix. -!- Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9). -!- The enzyme is activated by calcium. -!- Formerly EC 1.1.2.1 and EC 1.1.99.5. P18159 P18159 5.4.2.2 Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent). Glucose phosphomutase. Phosphoglucose mutase. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. -!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1. P18185 P18185 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. P19405 P19405 3.1.3.1 Alkaline phosphatase. Alkaline phosphomonoesterase. Glycerophosphatase. Phosphomonoesterase. A phosphate monoester + H(2)O = an alcohol + phosphate. Mg(2+); Zn(2+). -!- Active at a high pH optimum. -!- Wide specificity. -!- Also catalyzes transphosphorylations. -!- Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1). P19406 P19406 3.1.3.1 Alkaline phosphatase. Alkaline phosphomonoesterase. Glycerophosphatase. Phosphomonoesterase. A phosphate monoester + H(2)O = an alcohol + phosphate. Mg(2+); Zn(2+). -!- Active at a high pH optimum. -!- Wide specificity. -!- Also catalyzes transphosphorylations. -!- Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1). P19582 P19582 1.1.1.3 Homoserine dehydrogenase. L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H. -!- The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+). -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4. P19669 P19669 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. P20099 P20099 1.8.4.13 L-methionine (S)-S-oxide reductase. Acetylmethionine sulfoxide reductase. Free-methionine (S)-S-oxide reductase. FSMsr. Methionine sulfoxide reductase. Methionine-S-oxide reductase. Methyl sulfoxide reductase I and II. L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin. NADPH. -!- The reaction occurs in the opposite direction to that given above. -!- Dithiothreitol can replace reduced thioredoxin. -!- L-methionine (R)-S-oxide is not a substrate (see EC 1.8.4.14). -!- Formerly EC 1.8.4.5. P20166 P20166 2.7.1.199 Protein-N(pi)-phosphohistidine--D-glucose phosphotransferase. D-glucose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-glucose(Side 1) = [protein]-L- histidine + D-glucose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P20966 P20966 2.7.1.202 Protein-N(pi)-phosphohistidine--D-fructose phosphotransferase. Fructose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-fructose(Side 1) = [protein]-L- histidine + D-fructose 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P21165 P21165 3.4.13.9 Xaa-Pro dipeptidase. Gamma-peptidase. Imidodipeptidase. Peptidase D. Prolidase. Proline dipeptidase. X-Pro dipeptidase. Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro. Mn(2+). -!- Possibly thiol dependent. -!- Cytosolic from most animal tissues. -!- Belongs to peptidase family M24A. -!- Formerly EC 3.4.3.7. P21177 P21177 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase. Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase. (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. -!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211). P21177 P21177 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). P21177 P21177 5.1.2.3 3-hydroxybutyryl-CoA epimerase. (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. P21177 P21177 5.3.3.8 Delta(3)-Delta(2)-enoyl-CoA isomerase. 3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase. (1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. -!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters. P21189 P21189 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P21513 P21513 3.1.26.12 Ribonuclease E. Endoribonuclease E. RNase E. Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions. -!- RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication. -!- The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction. -!- 2'-O-methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5' to that locus. -!- In Escherichia coli, the enzyme is found in the RNA degradosome. -!- The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, EC 4.1.1.11 and EC 2.7.7.8. -!- Formerly EC 3.1.26.n1. P21599 P21599 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). P21873 P21873 1.2.4.1 Pyruvate dehydrogenase (acetyl-transferring). MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase. Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. P21879 P21879 1.1.1.205 IMP dehydrogenase. IMP oxidoreductase. Inosinate dehydrogenase. Inosine 5'-monophosphate dehydrogenase. Inosine monophosphate oxidoreductase. Inosinic acid dehydrogenase. Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH. -!- The enzyme acts on the hydroxy group of the hydrated derivative of the substrate. -!- Formerly EC 1.2.1.14. P21880 P21880 1.8.1.4 Dihydrolipoyl dehydrogenase. Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. FAD. -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3. P21882 P21882 1.2.4.1 Pyruvate dehydrogenase (acetyl-transferring). MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase. Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. P21883 P21883 2.3.1.12 Dihydrolipoyllysine-residue acetyltransferase. Acetyl-CoA:dihydrolipoamide S-acetyltransferase. Dihydrolipoamide S-acetyltransferase. Dihydrolipoate acetyltransferase. Dihydrolipoic transacetylase. Dihydrolipoyl acetyltransferase. Lipoate acetyltransferase. Lipoate transacetylase. Lipoic acetyltransferase. Lipoic acid acetyltransferase. Lipoic transacetylase. Lipoylacetyltransferase. Thioltransacetylase A. Transacetylase X. Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine. -!- A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A. P21885 P21885 4.1.1.19 Arginine decarboxylase. L-arginine carboxy-lyase. L-arginine = agmatine + CO(2). Pyridoxal 5'-phosphate. P21888 P21888 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). P21889 P21889 6.1.1.12 Aspartate--tRNA ligase. Aspartic acid translase. Aspartyl-tRNA synthetase. ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). P22106 P22106 6.3.5.4 Asparagine synthase (glutamine-hydrolyzing). AS-B. Asparagine synthetase (glutamine-hydrolyzing). Asparagine synthetase B. Glutamine-dependent asparagine synthetase. ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate. -!- The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel. -!- The enzyme catalyzes three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. -!- The C-terminal active site mediates both the synthesis of a beta- aspartyl-AMP intermediate and its subsequent reaction with ammonia. -!- The ammonia released is channeled to the other active site to yield asparagine. P22255 P22255 3.1.3.7 3'(2'),5'-bisphosphate nucleotidase. 3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase. 3'-phosphoadenylylsulfate 3'-phosphatase. DPNPase. Phosphoadenylate 3'-nucleotidase. Adenosine 3',5'-bisphosphate + H(2)O = adenosine 5'-phosphate + phosphate. -!- Also acts on 3'-phosphoadenylylsulfate, and on the corresponding 2'-phosphates. P22259 P22259 4.1.1.49 Phosphoenolpyruvate carboxykinase (ATP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2). P22326 P22326 6.1.1.1 Tyrosine--tRNA ligase. L-tyrosine-tRNA(Tyr) ligase (AMP-forming). Tyrosine translase. Tyrosine tRNA synthetase. Tyrosine-transfer ribonucleate synthetase. Tyrosine-transfer RNA ligase. Tyrosyl-transfer ribonucleate synthetase. Tyrosyl-transfer ribonucleic acid synthetase. Tyrosyl-transfer RNA synthetase. Tyrosyl-tRNA ligase. Tyrosyl-tRNA synthetase. ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). P22447 P22447 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P23129 P23129 1.2.4.2 Oxoglutarate dehydrogenase (succinyl-transferring). 2-ketoglutarate dehydrogenase. 2-oxoglutarate dehydrogenase. 2-oxoglutarate: lipoate oxidoreductase. 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- succinylating). AKGDH. Alpha-ketoglutarate dehydrogenase. Alpha-ketoglutaric acid dehydrogenase. Alpha-ketoglutaric dehydrogenase. Alpha-oxoglutarate dehydrogenase. Ketoglutaric dehydrogenase. OGDC. Oxoglutarate decarboxylase. Oxoglutarate dehydrogenase. Oxoglutarate dehydrogenase (lipoamide). 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61. P23353 P23353 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. P23388 P23388 2.7.3.9 Phosphoenolpyruvate--protein phosphotransferase. Enzyme I of the phosphotransferase system. Phosphoenolpyruvate sugar phosphotransferase enzyme I. Phosphoenolpyruvate--protein phosphatase. Phosphopyruvate--protein factor phosphotransferase. Phosphopyruvate--protein phosphotransferase. Sugar--PEP phosphotransferase enzyme I. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine. -!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. P23522 P23522 4.1.2.20 2-dehydro-3-deoxyglucarate aldolase. 2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase. 2-keto-3-deoxyglucarate aldolase. Alpha-keto-beta-deoxy-D-glucarate aldolase. 2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde. P23530 P23530 2.7.3.9 Phosphoenolpyruvate--protein phosphotransferase. Enzyme I of the phosphotransferase system. Phosphoenolpyruvate sugar phosphotransferase enzyme I. Phosphoenolpyruvate--protein phosphatase. Phosphopyruvate--protein factor phosphotransferase. Phosphopyruvate--protein phosphotransferase. Sugar--PEP phosphotransferase enzyme I. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine. -!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. P23538 P23538 2.7.9.2 Pyruvate, water dikinase. Phosphoenolpyruvate synthase. Pyruvate,water dikinase. ATP + pyruvate + H(2)O = AMP + phosphoenolpyruvate + phosphate. Mn(2+). P23545 P23545 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P23721 P23721 2.6.1.52 Phosphoserine transaminase. 3-phosphoserine aminotransferase. 3PHP transaminase. Hydroxypyruvic phosphate--glutamic transaminase. L-phosphoserine aminotransferase. Phosphohydroxypyruvate transaminase. Phosphohydroxypyruvic--glutamic transaminase. Phosphoserine aminotransferase. PSAT. (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + L-glutamate. Pyridoxal 5'-phosphate. -!- Catalyzes the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli. -!- Also catalyzes the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in E.coli (using reaction 2 above). -!- In E.coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). -!- Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis. -!- Non-phosphorylated forms of serine and threonine are not substrates. P23874 P23874 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P23893 P23893 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. P23966 P23966 4.1.3.36 1,4-dihydroxy-2-naphthoyl-CoA synthase. DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing). 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O. -!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzyme A group is subsequently removed from the product by EC 3.1.2.28. P23971 P23971 6.2.1.26 o-succinylbenzoate--CoA ligase. o-succinylbenzoyl-CoA synthetase. OSB-CoA synthetase. ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl- CoA. P24182 P24182 6.3.4.14 Biotin carboxylase. ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]- carboxybiotin-N(6)-L-lysine. -!- This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15. -!- In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). -!- Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyzes the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2). P24182 P24182 6.4.1.2 Acetyl-CoA carboxylase. ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA. Biotin. -!- This enzyme is a multi-domain polypeptide that catalyzes three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyzes the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. -!- In some organisms these activities are catalyzed by separate enzymes (see EC 6.3.4.14 and EC 2.1.3.15). -!- The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not. P24205 P24205 2.3.1.243 Lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase. Myristoyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)- (dodecanoyl)-lipid IV(A) O-myristoyltransferase. A tetradecanoyl-[acyl-carrier protein] + (Kdo)(2)-(dodecanoyl)-lipid IV(A) = Kdo(2)-lipid A + a holo-[acyl-carrier protein]. -!- The enzyme, characterized from the bacterium Escherichia coli, is involed in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. P24400 P24400 2.7.1.207 Protein-N(pi)-phosphohistidine--lactose phosphotransferase. Lactose PTS permease. [Protein]-N(pi)-phospho-L-histidine + lactose(Side 1) = [protein]-L- histidine + lactose 6'-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P24602 P24602 1.16.3.1 Ferroxidase. Ceruloplasmin. HEPH. Hephaestin. 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. Cu cation. P25151 P25151 6.1.1.1 Tyrosine--tRNA ligase. L-tyrosine-tRNA(Tyr) ligase (AMP-forming). Tyrosine translase. Tyrosine tRNA synthetase. Tyrosine-transfer ribonucleate synthetase. Tyrosine-transfer RNA ligase. Tyrosyl-transfer ribonucleate synthetase. Tyrosyl-transfer ribonucleic acid synthetase. Tyrosyl-transfer RNA synthetase. Tyrosyl-tRNA ligase. Tyrosyl-tRNA synthetase. ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). P25177 P25177 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. P25524 P25524 3.5.4.1 Cytosine deaminase. Cytosine aminohydrolase. Cytosine + H(2)O = uracil + NH(3). -!- Also acts on 5-methylcytosine. P25665 P25665 2.1.1.14 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. Cobalamin-independent methionine synthase. Homocysteine methylase. Methionine synthase (cobalamin-independent). Methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase. Tetrahydropteroylglutamate-homocysteine transmethylase. 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. Zn(2+). -!- Requires phosphate. -!- The enzyme from Escherichia coli also requires a reducing system. -!- Unlike EC 2.1.1.13 this enzyme does not contain cobalamin. P25906 P25906 1.1.1.65 Pyridoxine 4-dehydrogenase. PL reductase. Pyridoxal reductase. Pyridoxin dehydrogenase. Pyridoxine dehydrogenase. Pyridoxine + NADP(+) = pyridoxal + NADPH. -!- Also oxidizes pyridoxine phosphate. P25924 P25924 1.3.1.76 Precorrin-2 dehydrogenase. Precorrin-2 oxidase. Precorrin-2 + NAD(+) = sirohydrochlorin + NADH. -!- Catalyzes the second of three steps leading to the formation of siroheme from uroporphyrinogen III. -!- The first step involves the donation of two S-adenosyl-L-methionine- derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4). -!- In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. -!- In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction. P25924 P25924 2.1.1.107 Uroporphyrinogen-III C-methyltransferase. Adenosylmethionine-uroporphyrinogen III methyltransferase. S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase. SUMT. Urogen III methylase. Uroporphyrin-III C-methyltransferase. Uroporphyrinogen III methylase. Uroporphyrinogen methyltransferase. Uroporphyrinogen-III methylase. Uroporphyrinogen-III methyltransferase. 2 S-adenosyl-L-methionine + uroporphyrinogen III = 2 S-adenosyl-L- homocysteine + precorrin-2. -!- This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. -!- It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. -!- The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4). -!- In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. -!- In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction. -!- Also involved in the biosynthesis of cobalamin. P25924 P25924 4.99.1.4 Sirohydrochlorin ferrochelatase. Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). -!- This enzyme catalyzes the third of three steps leading to the formation of siroheme from uroporphyrinogen III. -!- The first step involves the donation of two S-adenosyl-L-methionine- derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76). -!- In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. -!- In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction. P25993 P25993 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. P25994 P25994 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. P26276 P26276 5.4.2.2 Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent). Glucose phosphomutase. Phosphoglucose mutase. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. -!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1. P26276 P26276 5.4.2.8 Phosphomannomutase. Phosphomannose mutase. Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. -!- Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.7. P26290 P26290 7.1.1.6 Plastoquinol--plastocyanin reductase. Cytochrome b6f complex. Plastoquinol + 2 oxidized plastocyanin + 2 H(+)(Side 1) = plastoquinone + 2 reduced plastocyanin + 4 H(+)(Side 2). -!- Contains two b-type cytochromes, two c-type cytochromes (c(n) and f), and a [2Fe-2S] Rieske cluster. -!- The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). -!- Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. -!- In chloroplasts, protons are translocated through the thylakoid membrane from the lumen to the stroma. -!- The mechanism occurs through the Q cycle as in EC 7.1.1.8 (complex III) and involves electron bifurcation. -!- Formerly EC 1.10.9.1 and EC 1.10.99.1. P26292 P26292 7.1.1.6 Plastoquinol--plastocyanin reductase. Cytochrome b6f complex. Plastoquinol + 2 oxidized plastocyanin + 2 H(+)(Side 1) = plastoquinone + 2 reduced plastocyanin + 4 H(+)(Side 2). -!- Contains two b-type cytochromes, two c-type cytochromes (c(n) and f), and a [2Fe-2S] Rieske cluster. -!- The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). -!- Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. -!- In chloroplasts, protons are translocated through the thylakoid membrane from the lumen to the stroma. -!- The mechanism occurs through the Q cycle as in EC 7.1.1.8 (complex III) and involves electron bifurcation. -!- Formerly EC 1.10.9.1 and EC 1.10.99.1. P26380 P26380 2.7.1.202 Protein-N(pi)-phosphohistidine--D-fructose phosphotransferase. Fructose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-fructose(Side 1) = [protein]-L- histidine + D-fructose 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P26527 P26527 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P26811 P26811 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P26899 P26899 4.3.1.1 Aspartate ammonia-lyase. Aspartase. Fumaric aminase. L-aspartate = fumarate + NH(3). P26900 P26900 3.5.1.1 Asparaginase. L-asparaginase. L-asparagine amidohydrolase. L-asparagine + H(2)O = L-aspartate + NH(3). P26901 P26901 1.11.1.6 Catalase. 2 H(2)O(2) = O(2) + 2 H(2)O. Heme; Mn(2+). -!- A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase. -!- The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. -!- Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21. P27179 P27179 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P27278 P27278 2.7.1.22 Ribosylnicotinamide kinase. ATP + 1-(beta-D-ribofuranosyl)-nicotinamide = ADP + beta-nicotinamide D-ribonucleotide. P27278 P27278 2.7.7.1 Nicotinamide-nucleotide adenylyltransferase. Adenosine triphosphate-nicotinamide mononucleotide transadenylase. Diphosphopyridine nucleotide pyrophosphorylase. NAD(+) diphosphorylase. NAD(+) pyrophosphorylase. Nicotinamide adenine dinucleotide pyrophosphorylase. Nicotinamide mononucleotide adenylyltransferase. NMN adenylyltransferase. NMNAT. ATP + nicotinamide ribonucleotide = diphosphate + NAD(+). -!- Nicotinate nucleotide can also act as acceptor. -!- See also EC 2.7.7.18. P27550 P27550 6.2.1.1 Acetate--CoA ligase. Acetate thiokinase. Acetyl-activating enzyme. Acetyl-CoA synthase. Acetyl-CoA synthetase. Acyl-activating enzyme. ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. -!- Also acts on propanoate and propenoate. P27830 P27830 4.2.1.46 dTDP-glucose 4,6-dehydratase. dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O. NAD(+). P27876 P27876 5.3.1.1 Triose-phosphate isomerase. Phosphotriose isomerase. Triose phosphoisomerase. Triosephosphate isomerase. Triosephosphate mutase. D-glyceraldehyde 3-phosphate = glycerone phosphate. P28008 P28008 2.7.1.197 Protein-N(pi)-phosphohistidine--D-mannitol phosphotransferase. D-mannitol PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-mannitol(Side 1) = [protein]-L- histidine + D-mannitol 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate--protein phosphotransferase). -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P28619 P28619 2.7.7.56 tRNA nucleotidyltransferase. Phosphate-dependent exonuclease. Ribonuclease PH. RNase PH. tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate. -!- Brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3'-terminus in tRNA and nucleoside diphosphate. -!- Not identical with EC 2.7.7.8. P28764 P28764 1.15.1.1 Superoxide dismutase. 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Fe cation or Mn(2+) or (Zn(2+) and Cu cation). P28904 P28904 3.2.1.93 Alpha,alpha-phosphotrehalase. Trehalose-6-phosphate hydrolase. Alpha,alpha-trehalose 6-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate. P29107 P29107 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. P29254 P29254 1.97.1.12 Photosystem I. Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin. -!- Contains chlorophyll, phylloquinones, carotenoids and [4Fe-4S] clusters. -!- Cytochrome c6 can act as an alternative electron donor, and flavodoxin as an alternative acceptor in some species. P29255 P29255 1.97.1.12 Photosystem I. Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin. -!- Contains chlorophyll, phylloquinones, carotenoids and [4Fe-4S] clusters. -!- Cytochrome c6 can act as an alternative electron donor, and flavodoxin as an alternative acceptor in some species. P29726 P29726 6.3.4.4 Adenylosuccinate synthase. Adenylosuccinate synthetase. IMP--aspartate ligase. Succinoadenylic kinosynthetase. GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)- AMP. P29727 P29727 6.3.5.2 GMP synthase (glutamine-hydrolyzing). GMP synthetase (glutamine-hydrolyzing). ATP + XMP + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate. -!- Involved in the de novo biosynthesis of guanosine nucleotides. -!- An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. -!- The enzyme can catalyze the second reaction alone in the presence of ammonia. -!- Formerly EC 6.3.4.1. P30011 P30011 2.4.2.19 Nicotinate-nucleotide diphosphorylase (carboxylating). Nicotinate-nucleotide pyrophosphorylase (carboxylating). Quinolinate phosphoribosyltransferase (decarboxylating). Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3- dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate. -!- The reaction is catalyzed in the opposite direction. -!- Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD(+) biosynthesis enzyme shared by both eukaryotes and prokaryotes. P30125 P30125 1.1.1.85 3-isopropylmalate dehydrogenase. Beta-IPM dehydrogenase. Beta-isopropylmalate dehydrogenase. IMDH. (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH. P30870 P30870 2.7.7.42 [Glutamine synthetase] adenylyltransferase. [Glutamate--ammonia-ligase] adenylyltransferase. Glutamate-ammonia-ligase adenylyltransferase. Glutamine-synthetase adenylyltransferase. ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine. -!- This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89). -!- The two activities are present on separate domains. P30870 P30870 2.7.7.89 [Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase. [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP. -!- This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42). -!- The two activities are present on separate domains. -!- Formerly EC 3.1.4.15. P30871 P30871 3.6.1.25 Triphosphatase. Triphosphate + H(2)O = diphosphate + phosphate. P30949 P30949 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. P30950 P30950 4.2.1.24 Porphobilinogen synthase. Aminolevulinate dehydratase. Delta-aminolevulinic acid dehydratase. 2 5-aminolevulinate = porphobilinogen + 2 H(2)O. Zn(2+). -!- The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. -!- The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. -!- In humans, the enzyme is a primary target for the environmental toxin Pb. -!- The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation. P31103 P31103 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. P31104 P31104 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. P31112 P31112 2.5.1.30 Heptaprenyl diphosphate synthase. All-trans-heptaprenyl-diphosphate synthase. HepPP synthase. Heptaprenyl pyrophosphate synthetase. Trans-hexaprenyltranstransferase. (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate. -!- This enzyme catalyzes the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. -!- The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry. P31114 P31114 2.5.1.30 Heptaprenyl diphosphate synthase. All-trans-heptaprenyl-diphosphate synthase. HepPP synthase. Heptaprenyl pyrophosphate synthetase. Trans-hexaprenyltranstransferase. (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate. -!- This enzyme catalyzes the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. -!- The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry. P31120 P31120 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. P31142 P31142 2.8.1.2 3-mercaptopyruvate sulfurtransferase. 3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin. Zn(2+). -!- The enzyme catalyzes a transsulfuration reaction from 3-mercaptopyruvate to an internal cysteine residue. -!- In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. -!- The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11). P31572 P31572 2.8.3.21 L-carnitine CoA-transferase. (1) (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4- (trimethylammonio)but-2-enoate + L-carnitinyl-CoA. (2) 4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA. -!- The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. -!- It has similar activity with both substrates. -!- Formerly EC 4.2.1.89. P31658 P31658 3.5.1.124 Protein deglycase. Glyoxylase III. (1) An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H(2)O = a [protein]-L-arginine + lactate. (2) An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate. (3) An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H(2)O = a [protein]-L-cysteine + lactate. -!- The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. -!- The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. -!- The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively. P31658 P31658 4.2.1.130 D-lactate dehydratase. Glyoxylase III. (R)-lactate = methylglyoxal + H(2)O. -!- The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. -!- The other known route for this conversion is the two-step GSH- dependent pathway catalyzed by EC 4.4.1.5 and EC 3.1.2.6. P31663 P31663 6.3.2.1 Pantoate--beta-alanine ligase (AMP-forming). Pantoate-activating enzyme. Pantoic-activating enzyme. Pantothenate synthetase. ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. P31973 P31973 1.18.1.2 Ferredoxin--NADP(+) reductase. 2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH. FAD. -!- In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin. -!- Formerly EC 1.6.7.1 and EC 1.6.99.4. P32397 P32397 1.3.3.4 Protoporphyrinogen oxidase. Protoporphyrinogen IX oxidase. Protoporphyrinogenase. Protoporphyrinogen-IX + 3 O(2) = protoporphyrin-IX + 3 H(2)O(2). FAD. -!- Also slowly oxidizes mesoporphyrinogen IX. P32422 P32422 1.97.1.12 Photosystem I. Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin. -!- Contains chlorophyll, phylloquinones, carotenoids and [4Fe-4S] clusters. -!- Cytochrome c6 can act as an alternative electron donor, and flavodoxin as an alternative acceptor in some species. P32670 P32670 2.7.1.202 Protein-N(pi)-phosphohistidine--D-fructose phosphotransferase. Fructose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-fructose(Side 1) = [protein]-L- histidine + D-fructose 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P32670 P32670 2.7.3.9 Phosphoenolpyruvate--protein phosphotransferase. Enzyme I of the phosphotransferase system. Phosphoenolpyruvate sugar phosphotransferase enzyme I. Phosphoenolpyruvate--protein phosphatase. Phosphopyruvate--protein factor phosphotransferase. Phosphopyruvate--protein phosphotransferase. Sugar--PEP phosphotransferase enzyme I. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine. -!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. P33195 P33195 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. P33197 P33197 1.1.1.42 Isocitrate dehydrogenase (NADP(+)). Dual-cofactor-specific isocitrate dehydrogenase. IDH. IDP. Isocitrate (NADP) dehydrogenase. Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Isocitrate dehydrogenase (NADP). Isocitrate dehydrogenase (NADP-dependent). NADP isocitric dehydrogenase. NADP(+)-ICDH. NADP(+)-IDH. NADP(+)-linked isocitrate dehydrogenase. NADP-dependent isocitrate dehydrogenase. NADP-dependent isocitric dehydrogenase. NADP-linked isocitrate dehydrogenase. NADP-specific isocitrate dehydrogenase. Oxalosuccinate decarboxylase. Oxalsuccinic decarboxylase. Triphosphopyridine nucleotide-linked isocitrate dehydrogenase- oxalosuccinate carboxylase. Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Mn(2+) or Mg(2+). -!- Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate. -!- In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. -!- The enzyme from some species can also use NAD(+) but much more slowly. P33380 P33380 1.1.1.27 L-lactate dehydrogenase. L-lactic acid dehydrogenase. L-lactic dehydrogenase. (S)-lactate + NAD(+) = pyruvate + NADH. -!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme. P33919 P33919 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P35136 P35136 1.1.1.95 Phosphoglycerate dehydrogenase. 3-phosphoglycerate dehydrogenase. 3-phosphoglyceric acid dehydrogenase. 3PHP reductase. Alpha-KG reductase. Alpha-phosphoglycerate dehydrogenase. D-3-phosphoglycerate dehydrogenase. Glycerate 3-phosphate dehydrogenase. Glycerate-1,3-phosphate dehydrogenase. PGDH. Phosphoglycerate oxidoreductase. Phosphoglyceric acid dehydrogenase. 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. -!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399. P35136 P35136 1.1.1.399 2-oxoglutarate reductase. (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. -!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95. P36430 P36430 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). P36672 P36672 2.7.1.201 Protein-N(pi)-phosphohistidine--trehalose phosphotransferase. Trehalose PTS permease. [Protein]-N(pi)-phospho-L-histidine + alpha,alpha-trehalose(Side 1) = [protein]-L-histidine + alpha,alpha-trehalose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P36683 P36683 4.2.1.3 Aconitate hydratase. Aconitase. Cis-aconitase. Citrate hydro-lyase. Citrate(isocitrate) hydro-lyase. Citrate = isocitrate. Iron-sulfur. -!- Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. -!- The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. -!- Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3- tricarboxylate. -!- Formerly EC 4.2.1.4. P36683 P36683 4.2.1.99 2-methylisocitrate dehydratase. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3- tricarboxylate + H(2)O. -!- The enzyme from the fungus Yarrowia lipolytica does not act on isocitrate. P36938 P36938 5.4.2.2 Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent). Glucose phosphomutase. Phosphoglucose mutase. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. -!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1. P36945 P36945 2.7.1.15 Ribokinase. ATP + D-ribose = ADP + D-ribose 5-phosphate. -!- 2-deoxy-D-ribose can also act as acceptor. P36947 P36947 3.6.3.17 Monosaccharide-transporting ATPase. ATP + H(2)O + monosaccharide(Out) = ADP + phosphate + monosaccharide(In). -!- Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside. P37095 P37095 3.4.11.23 PepB aminopeptidase. Aminopeptidase B. Peptidase B. Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln. -!- A 270-kDa protein composed of six 46.3-kDa subunits. -!- The pH optimum is in the alkaline range and activity is stimulated by KCl. -!- Belongs to peptidase family M17. P37101 P37101 2.7.1.19 Phosphoribulokinase. Phosphopentokinase. ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate. P37146 P37146 1.17.4.1 Ribonucleoside-diphosphate reductase. Ribonucleotide reductase. 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Fe(3+) or adenosylcob(III)alamin or Mn(2+). -!- This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. -!- There are three types of this enzyme differing in their cofactors. -!- Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. -!- In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6 and EC 1.17.4.2. P37177 P37177 2.7.3.9 Phosphoenolpyruvate--protein phosphotransferase. Enzyme I of the phosphotransferase system. Phosphoenolpyruvate sugar phosphotransferase enzyme I. Phosphoenolpyruvate--protein phosphatase. Phosphopyruvate--protein factor phosphotransferase. Phosphopyruvate--protein phosphotransferase. Sugar--PEP phosphotransferase enzyme I. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine. -!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. P37188 P37188 2.7.1.200 Protein-N(pi)-phosphohistidine--galactitol phosphotransferase. Galactitol PTS permease. [Protein]-N(pi)-phospho-L-histidine + galactitol(Side 1) = [protein]-L- histidine + galactitol 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P37251 P37251 2.2.1.6 Acetolactate synthase. Acetohydroxy acid synthetase. Acetohydroxyacid synthase. Acetolactate pyruvate-lyase (carboxylating). Acetolactic synthetase. Alpha-acetohydroxy acid synthetase. Alpha-acetohydroxyacid synthase. Alpha-acetolactate synthase. Alpha-acetolactate synthetase. 2 pyruvate = 2-acetolactate + CO(2). Thiamine diphosphate. -!- The reaction shown is in the pathway of biosynthesis of valine. -!- The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine. -!- Formerly EC 4.1.3.18. P37253 P37253 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. P37330 P37330 2.3.3.9 Malate synthase. Glyoxylate transacetase. Glyoxylate transacetylase. Glyoxylic transacetase. L-malate glyoxylate-lyase (CoA-acetylating). Malate condensing enzyme. Malate synthetase. Malic synthetase. Malic-condensing enzyme. Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA. -!- The enzyme catalyzes the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. -!- Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO(2). -!- Formerly EC 4.1.3.2. P37349 P37349 2.7.1.121 Phosphoenolpyruvate--glycerone phosphotransferase. Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate. P37464 P37464 6.1.1.11 Serine--tRNA ligase. Serine translase. SerRS. Seryl-transfer ribonucleate synthetase. Seryl-transfer ribonucleic acid synthetase. Seryl-transfer RNA synthetase. Seryl-tRNA synthetase. (1) ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). (2) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). -!- This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1. P37465 P37465 6.1.1.10 Methionine--tRNA ligase. Methionine translase. Methionyl-transfer ribonucleate synthetase. Methionyl-transfer ribonucleic acid synthetase. Methionyl-transfer RNA synthetase. Methionyl-tRNA synthetase. MetRS. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl- tRNA(Met). -!- In those organisms producing N-formylmethionyl-tRNA(fMet) for translation initiation, this enzyme also recognizes the initiator tRNA(fMet) and catalyzes the formation of L-methionyl-tRNA(fMet), the substrate for EC 2.1.2.9. P37477 P37477 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). P37487 P37487 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P37527 P37527 4.3.3.6 Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing). D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate. -!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants. P37552 P37552 3.5.99.10 2-iminobutanoate/2-iminopropanoate deaminase. Enamine/imine deaminase. (1) 2-iminobutanoate + H(2)O = 2-oxobutanoate + NH(3). (2) 2-iminopropanoate + H(2)O = pyruvate + NH(3). -!- This enzyme, which has been found in all species and tissues examined, catalyzes the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19 and EC 4.3.1.17. -!- The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates. P37562 P37562 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P37570 P37570 2.7.14.1 Protein arginine kinase. ATP + a [protein]-L-arginine = ADP + a [protein]-N(omega)-phospho-L- arginine. -!- The enzyme, characterized from Gram-positive bacteria, is involved in the regulation of the bacterial stress response. P37666 P37666 1.1.1.79 Glyoxylate reductase (NADP(+)). Glycolate + NADP(+) = glyoxylate + NADPH. -!- Also reduces hydroxypyruvate to glycerate. -!- Has some affinity for NAD(+). P37666 P37666 1.1.1.81 Hydroxypyruvate reductase. D-glycerate dehydrogenase. D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H. P37666 P37666 1.1.1.215 Gluconate 2-dehydrogenase. 2-keto-D-gluconate reductase. 2-ketogluconate reductase. D-gluconate + NADP(+) = 2-dehydro-D-gluconate + NADPH. -!- Also acts on L-idonate, D-galactonate and D-xylonate. P37689 P37689 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. P37744 P37744 2.7.7.24 Glucose-1-phosphate thymidylyltransferase. dTDP-glucose diphosphorylase. dTDP-glucose pyrophosphorylase. dTDP-glucose synthase. dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose. P37747 P37747 5.4.99.9 UDP-galactopyranose mutase. UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose. P37755 P37755 5.4.2.8 Phosphomannomutase. Phosphomannose mutase. Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. -!- Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.7. P37756 P37756 1.1.1.44 Phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating). 6-phosphogluconic carboxylase. 6-phosphogluconic dehydrogenase. 6PGD. Phosphogluconic acid dehydrogenase. 6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH. -!- The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. -!- Highly specific for NADP(+). -!- Cf. EC 1.1.1.343. P37759 P37759 4.2.1.46 dTDP-glucose 4,6-dehydratase. dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O. NAD(+). P37777 P37777 4.2.1.46 dTDP-glucose 4,6-dehydratase. dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O. NAD(+). P37779 P37779 2.7.7.24 Glucose-1-phosphate thymidylyltransferase. dTDP-glucose diphosphorylase. dTDP-glucose pyrophosphorylase. dTDP-glucose synthase. dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose. P37793 P37793 3.5.4.19 Phosphoribosyl-AMP cyclohydrolase. 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1-(5-phospho-beta-D-ribosyl)- 5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4- carboxamide. -!- The Neurospora crassa enzyme also catalyzes the reactions of EC 1.1.1.23 and EC 3.6.1.31. P37793 P37793 3.6.1.31 Phosphoribosyl-ATP diphosphatase. Phosphoribosyl-ATP pyrophosphatase. Phosphoribosyladenosine triphosphate pyrophosphatase. 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1-(5-phospho-beta-D-ribosyl)- AMP + diphosphate. -!- The Neurospora crassa enzyme also catalyzes the reactions of EC 1.1.1.23 and EC 3.5.4.19. P37808 P37808 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P37820 P37820 2.7.7.13 Mannose-1-phosphate guanylyltransferase. GDP-mannose pyrophosphorylase. GTP-mannose-1-phosphate guanylyltransferase. GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose. -!- The bacterial enzyme can also use ITP and dGTP as donors. P37869 P37869 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. P37870 P37870 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P37871 P37871 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P37877 P37877 2.7.2.1 Acetate kinase. Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK. ATP + acetate = ADP + acetyl phosphate. Mg(2+). -!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. P37940 P37940 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring). 2-oxoisocaproate dehydrogenase. 2-oxoisovalerate (lipoate) dehydrogenase. 3-methyl-2-oxobutanoate dehydrogenase (lipoamide). 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating). Alpha-keto-alpha-methylvalerate dehydrogenase. Alpha-ketoisocaproate dehydrogenase. Alpha-ketoisocaproic dehydrogenase. Alpha-ketoisocaproic-alpha-keto-alpha-methylvaleric dehydrogenase. Alpha-ketoisovalerate dehydrogenase. Alpha-oxoisocaproate dehydrogenase. BCKDH. BCOAD. Branched chain keto acid dehydrogenase. Branched-chain (-2-oxoacid) dehydrogenase (BCD). Branched-chain 2-keto acid dehydrogenase. Branched-chain 2-oxo acid dehydrogenase. Branched-chain alpha-keto acid dehydrogenase. Branched-chain alpha-oxo acid dehydrogenase. Branched-chain keto acid dehydrogenase. Branched-chain ketoacid dehydrogenase. Dehydrogenase, 2-oxoisovalerate (lipoate). Dehydrogenase, branched chain alpha-keto acid. 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine- residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2- oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. -!- It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168. -!- Formerly EC 1.2.4.3. P37946 P37946 4.3.1.19 Threonine ammonia-lyase. L-serine dehydratase. L-threonine deaminase. L-threonine dehydratase. L-threonine hydro-lyase (deaminating). Serine deaminase. Threonine deaminase. Threonine dehydrase. Threonine dehydratase. L-threonine = 2-oxobutanoate + NH(3). Pyridoxal 5'-phosphate or iron-sulfur. -!- The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond. -!- The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10. -!- The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17. -!- Formerly EC 4.2.1.16. P37949 P37949 3.6.5.n1 Elongation factor 4. GTP + H(2)O = GDP + phosphate. -!- The enzyme is required for accurate and efficient protein synthesis under certain stress conditions. -!- May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. -!- Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. -!- Binds to ribosomes in a GTP-dependent manner. P38021 P38021 2.6.1.13 Ornithine aminotransferase. L-ornithine 5-aminotransferase. L-ornithine aminotransferase. Ornithine 5-aminotransferase. Ornithine delta-transaminase. Ornithine ketoacid aminotransferase. Ornithine transaminase. Ornithine--2-oxoacid aminotransferase. Ornithine--alpha-ketoglutarate aminotransferase. Ornithine--keto acid aminotransferase. Ornithine--keto acid transaminase. Ornithine--ketoglutarate aminotransferase. Ornithine--oxo acid aminotransferase. Ornithine--oxo-acid transaminase. L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid. Pyridoxal 5'-phosphate. P38032 P38032 1.4.3.16 L-aspartate oxidase. LASPO. L-aspartate + O(2) = iminosuccinate + H(2)O(2). FAD. -!- L-aspartate oxidase catalyzes the first step in the de novo biosynthesis of NAD(+) in some bacteria. -!- O(2) can be replaced by fumarate as electron acceptor, yielding succinate. -!- The ability of the enzyme to use both O(2) and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions. -!- Iminosuccinate can either be hydrolyzed to form oxaloacetate and NH(3) or can be used by EC 2.5.1.72 in the production of quinolinate. P38033 P38033 2.8.1.7 Cysteine desulfurase. Cysteine desulfurylase. L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. Pyridoxal 5'-phosphate. -!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. P38038 P38038 1.8.1.2 Assimilatory sulfite reductase (NADPH). Sulfite reductase (NADPH). H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. FAD; FMN; Iron-sulfur; Siroheme. -!- The enzyme, which catalyzes the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. -!- Different from EC 1.8.99.5, which is involved in prokaryotic sulfur- based energy metabolism. -!- Formerly EC 1.8.99.1. P38051 P38051 5.4.4.2 Isochorismate synthase. Isochorismate mutase. Isochorismate synthetase. Chorismate = isochorismate. Mg(2+). -!- The reaction is reversible. -!- Formerly EC 5.4.99.6. P38576 P38576 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P39120 P39120 2.3.3.16 Citrate synthase (unknown stereospecificity). Citrate condensing enzyme. Citrate synthetase. Citric synthase. Citric-condensing enzyme. Citrogenase. CoA-acetylating citrate oxaloacetate-lyase. Condensing enzyme. Oxalacetic transacetase. Oxaloacetate transacetase. Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. -!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3). P39121 P39121 4.1.2.4 Deoxyribose-phosphate aldolase. 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase. Deoxyriboaldolase. Phosphodeoxyriboaldolase. 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. P39123 P39123 2.4.1.1 Glycogen phosphorylase. Amylophosphorylase. Muscle phosphorylase a and b. Polyphosphorylase. ((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. -!- This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. -!- Some of these enzymes catalyze the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. -!- The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. -!- The description (accepted name) of the enzyme should be modified for each specific instance by substituting 'glycogen' with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc. P39126 P39126 1.1.1.42 Isocitrate dehydrogenase (NADP(+)). Dual-cofactor-specific isocitrate dehydrogenase. IDH. IDP. Isocitrate (NADP) dehydrogenase. Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Isocitrate dehydrogenase (NADP). Isocitrate dehydrogenase (NADP-dependent). NADP isocitric dehydrogenase. NADP(+)-ICDH. NADP(+)-IDH. NADP(+)-linked isocitrate dehydrogenase. NADP-dependent isocitrate dehydrogenase. NADP-dependent isocitric dehydrogenase. NADP-linked isocitrate dehydrogenase. NADP-specific isocitrate dehydrogenase. Oxalosuccinate decarboxylase. Oxalsuccinic decarboxylase. Triphosphopyridine nucleotide-linked isocitrate dehydrogenase- oxalosuccinate carboxylase. Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Mn(2+) or Mg(2+). -!- Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate. -!- In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. -!- The enzyme from some species can also use NAD(+) but much more slowly. P39138 P39138 3.5.3.1 Arginase. Arginine amidinase. Canavanase. L-arginine + H(2)O = L-ornithine + urea. Mn(2+). -!- Also hydrolyzes alpha-N-substituted L-arginines and canavanine. P39145 P39145 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P39148 P39148 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. P39149 P39149 2.4.2.9 Uracil phosphoribosyltransferase. UMP diphosphorylase. UMP pyrophosphorylase. UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. P39463 P39463 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P39464 P39464 2.5.1.29 Geranylgeranyl diphosphate synthase. Farnesyltransferase. Farnesyltranstransferase. Geranylgeranyl pyrophosphate synthase. Geranylgeranyl pyrophosphate synthetase. Geranylgeranyl-diphosphate synthase. Geranylgeranyl-PP synthetase. (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate. -!- Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors. P39466 P39466 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P39471 P39471 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P39604 P39604 2.4.1.129 Peptidoglycan glycosyltransferase. Bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)- pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D- glucosaminyltransferase. Penicillin binding protein (3 or 1B). Peptidoglycan TGase. Peptidoglycan transglycosylase. PG-II. (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)- diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala- gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate. -!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. -!- Involved in the synthesis of cell-wall peptidoglycan. P39605 P39605 1.5.1.38 FMN reductase (NADPH). Flavin reductase P. FMNH(2) + NADP(+) = FMN + NADPH. FMN. -!- The enzymes from bioluminescent bacteria contain FMN, while the enzyme from Escherichia coli does not. -!- The enzyme often forms a two-component system with monooxygenases such as luciferase. -!- Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor. -!- While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity. -!- Formerly EC 1.5.1.29 and EC 1.6.8.1. P39610 P39610 2.7.1.35 Pyridoxal kinase. Pyridoxamine kinase. Pyridoxine kinase. Vitamin B(6) kinase. Vitamin B6 kinase. ATP + pyridoxal = ADP + pyridoxal 5'-phosphate. -!- Pyridoxine, pyridoxamine and various derivatives can also act as acceptors. P39633 P39633 1.4.1.2 Glutamate dehydrogenase. Glutamic dehydrogenase. L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH. P39634 P39634 1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenase. 1-pyrroline-5-carboxylate dehydrogenase. Delta(1)-pyrroline-5-carboxylate dehydrogenase. Pyrroline-5-carboxylate dehydrogenase. L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH. -!- This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. -!- (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. -!- In many bacterial species, both activities are carried out by a single bifunctional enzyme. -!- The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. -!- NADP(+) can also act as acceptor, but with lower activity. -!- Formerly EC 1.5.1.12. P39646 P39646 2.3.1.8 Phosphate acetyltransferase. Phosphoacylase. Phosphotransacetylase. Acetyl-CoA + phosphate = CoA + acetyl phosphate. -!- Also acts with other short-chain acyl-CoAs. P39764 P39764 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P39765 P39765 2.4.2.9 Uracil phosphoribosyltransferase. UMP diphosphorylase. UMP pyrophosphorylase. UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. P39773 P39773 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. P39794 P39794 2.7.1.201 Protein-N(pi)-phosphohistidine--trehalose phosphotransferase. Trehalose PTS permease. [Protein]-N(pi)-phospho-L-histidine + alpha,alpha-trehalose(Side 1) = [protein]-L-histidine + alpha,alpha-trehalose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P39812 P39812 1.4.1.13 Glutamate synthase (NADPH). Glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase. Glutamate synthetase (NADP). Glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP). Glutamine-ketoglutaric aminotransferase. GOGAT. L-glutamate synthase. L-glutamate synthetase. NADPH-dependent glutamate synthase. NADPH-glutamate synthase. 2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH. FAD; FMN; Iron-sulfur. -!- The reaction takes place in the opposite direction. -!- The protein is composed of two subunits, alpha and beta. -!- The alpha subunit is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4). -!- The beta subunit transfers electrons to the cosubstrate. -!- The NH(3) is channeled through a 31 A channel in the active protein. -!- In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can be produced. -!- In the intact alpha-beta complex, ammonia production only takes place as part of the overall reaction. -!- Formerly EC 2.6.1.53. P39821 P39821 1.2.1.41 Glutamate-5-semialdehyde dehydrogenase. Beta-glutamylphosphate reductase. Gamma-glutamylphosphate reductase. Glutamyl-gamma-semialdehyde dehydrogenase. L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH. P39912 P39912 2.5.1.54 3-deoxy-7-phosphoheptulonate synthase. 2-dehydro-3-deoxy-phosphoheptonate aldolase. 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). D-erythrose-4-phosphate-lyase. D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating). DAH7-P synthase. DAHP synthase. Deoxy-D-arabino-heptulosonate-7-phosphate synthetase. DHAP synthase. DS-Co. DS-Mn. KDPH synthase. KDPH synthetase. Phospho-2-dehydro-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptanoate aldolase. Phospho-2-keto-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptonic aldolase. Phospho-2-oxo-3-deoxyheptonate aldolase. Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D- arabino-hept-2-ulosonate 7-phosphate + phosphate. -!- Formerly EC 4.1.2.15. P39912 P39912 5.4.99.5 Chorismate mutase. Hydroxyphenylpyruvate synthase. Chorismate = prephenate. P40191 P40191 2.7.1.35 Pyridoxal kinase. Pyridoxamine kinase. Pyridoxine kinase. Vitamin B(6) kinase. Vitamin B6 kinase. ATP + pyridoxal = ADP + pyridoxal 5'-phosphate. -!- Pyridoxine, pyridoxamine and various derivatives can also act as acceptors. P40758 P40758 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P40924 P40924 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. P42085 P42085 2.4.2.22 Xanthine phosphoribosyltransferase. Xan phosphoribosyltransferase. Xanthine-guanine phosphoribosyltransferase. Xanthosine 5'-phosphate pyrophosphorylase. Xanthylate pyrophosphorylase. Xanthylic pyrophosphorylase. XMP pyrophosphorylase. XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine. P42175 P42175 1.7.5.1 Nitrate reductase (quinone). Dissimilatory nitrate reductase. Nitrate reductase A. Nitrate reductase Z. Quinol-nitrate oxidoreductase. Quinol/nitrate oxidoreductase. Nitrate + a quinol = nitrite + a quinone + H(2)O. Heme; Iron-sulfur; Molybdopterin guanine dinucleotide. -!- A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits. P42234 P42234 1.11.1.6 Catalase. 2 H(2)O(2) = O(2) + 2 H(2)O. Heme; Mn(2+). -!- A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase. -!- The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. -!- Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21. P42403 P42403 3.2.1.86 6-phospho-beta-glucosidase. Phospho-beta-glucosidase. Phosphocellobiase. 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H(2)O = D-glucose + D-glucose 6-phosphate. -!- Also hydrolyzes several other phospho-beta-D-glucosides, but not their non-phosphorylated forms. P42412 P42412 1.2.1.27 Methylmalonate-semialdehyde dehydrogenase (CoA acylating). Methylmalonate-semialdehyde dehydrogenase (acylating). MMSA dehydrogenase. MSDH. 2-methyl-3-oxopropanoate + CoA + H(2)O + NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH. -!- Also converts 3-oxopropanoate into acetyl-CoA. -!- The reaction occurs in two steps with the decarboxylation process preceding CoA-binding. -!- Bicarbonate rather than CO(2) is released as a final product. P42420 P42420 4.1.2.29 5-dehydro-2-deoxyphosphogluconate aldolase. 5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase. Phospho-5-dehydro-2-deoxygluconate aldolase. Phospho-5-keto-2-deoxygluconate aldolase. 5-dehydro-2-deoxy-D-gluconate 6-phosphate = glycerone phosphate + malonate semialdehyde. P42588 P42588 2.6.1.82 Putrescine--2-oxoglutarate transaminase. PAT. Putrescine aminotransferase. Putrescine transaminase. Putrescine-alpha-ketoglutarate transaminase. Putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H(2)O. Pyridoxal 5'-phosphate. -!- The enzymatic part of the reaction produces 4-aminobutanal that spontaneously cyclizes to form 1-pyrroline, which is a substrate for EC 1.2.1.19. -!- Cadaverine and spermidine can also act as substrates. -!- Forms part of the arginine catabolism pathway. -!- Cf. EC 2.6.1.113. P42632 P42632 2.3.1.54 Formate C-acetyltransferase. Pyruvate formate-lyase. Acetyl-CoA + formate = CoA + pyruvate. P42784 P42784 3.4.21.102 C-terminal processing peptidase. Photosystem II D1 protein processing peptidase. Protease Re. Tail-specific protease. Tsp protease. The enzyme shows specific recognition of a C-terminal tripeptide, Xaa- Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala- Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. -!- In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II; this proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. -!- Belongs to peptidase family S41. P42974 P42974 1.6.99.3 NADH dehydrogenase. Beta-NADH dehydrogenase dinucleotide. Cytochrome c reductase. Diaphorase. Dihydrocodehydrogenase I dehydrogenase. Dihydronicotinamide adenine dinucleotide dehydrogenase. Diphosphopyrinase. DPNH diaphorase. NADH diaphorase. NADH hydrogenase. NADH oxidoreductase. NADH-menadione oxidoreductase. NADH:cytochrome c oxidoreductase. Reduced diphosphopyridine nucleotide diaphorase. Type 1 dehydrogenase. Type I dehydrogenase. NADH + acceptor = NAD(+) + reduced acceptor. Flavoprotein; Iron-sulfur. -!- After preparations have been subjected to certain treatments cytochrome c may act as acceptor. -!- Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. -!- Present in a mitochondrial complex as EC 7.1.1.2. -!- Formerly EC 1.6.2.1. P43891 P43891 2.7.4.22 UMP kinase. UMP-kinase. UMPK. Uridine monophosphate kinase. Uridylate kinase. ATP + UMP = ADP + UDP. -!- Strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme EC 2.7.4.14 for the same purpose. -!- Subject of feedback regulation, being inhibited by UTP and activated by GTP. P45359 P45359 2.3.1.9 Acetyl-CoA C-acetyltransferase. Acetoacetyl-CoA thiolase. 2 acetyl-CoA = CoA + acetoacetyl-CoA. -!- The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. -!- In the second step the acyl group is transferred to an acetyl-CoA molecule. -!- Cf. EC 2.3.1.16. P45395 P45395 5.3.1.13 Arabinose-5-phosphate isomerase. Arabinose phosphate isomerase. Phosphoarabinoisomerase. D-arabinose 5-phosphate = D-ribulose 5-phosphate. -!- The enzyme is involved in the pathway for synthesis of 3-deoxy-D- manno-octulosonate (Kdo), a component of bacterial lipopolysaccharides and plant call walls. P45425 P45425 2.7.1.60 N-acylmannosamine kinase. ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate. -!- Acts on the acetyl and glycolyl derivatives. P45523 P45523 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. P45578 P45578 4.4.1.21 S-ribosylhomocysteine lyase. S-ribosylhomocysteinase. S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5- dihydroxypentan-2,3-dione. Fe(2+). -!- The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density. -!- Formerly EC 3.2.1.148 and EC 3.3.1.3. P45694 P45694 2.2.1.1 Transketolase. Glycoaldehyde transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. Thiamine diphosphate. -!- Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH. -!- The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor. P45740 P45740 4.1.99.17 Phosphomethylpyrimidine synthase. 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO. Iron-sulfur. -!- Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. -!- The first stage of catalysis is reduction of the S-adenosyl-L- methionine to produce L-methionine and a 5'-deoxyadenosin-5'-yl radical that is crucial for the conversion of the substrate. -!- Part of the pathway for thiamine biosynthesis. P45744 P45744 5.4.4.2 Isochorismate synthase. Isochorismate mutase. Isochorismate synthetase. Chorismate = isochorismate. Mg(2+). -!- The reaction is reversible. -!- Formerly EC 5.4.99.6. P46215 P46215 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). P46353 P46353 5.4.2.7 Phosphopentomutase. Deoxyribomutase. Deoxyribose phosphomutase. Phosphodeoxyribomutase. Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. -!- Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D- ribose 5-phosphate. -!- Alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5- bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.6. P46354 P46354 2.4.2.1 Purine-nucleoside phosphorylase. Inosine phosphorylase. PNPase. (1) Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. (2) Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate. -!- Specificity not completely determined. -!- Can also catalyze ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5. P48372 P48372 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P48576 P48576 2.3.3.13 2-isopropylmalate synthase. 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating). Alpha-IPM synthetase. Alpha-isopropylmalate synthase. Alpha-isopropylmalate synthetase. Alpha-isopropylmalic synthetase. Isopropylmalate synthase. Isopropylmalate synthetase. Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA. K(+). -!- Formerly EC 4.1.3.12. P49057 P49057 6.3.5.2 GMP synthase (glutamine-hydrolyzing). GMP synthetase (glutamine-hydrolyzing). ATP + XMP + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate. -!- Involved in the de novo biosynthesis of guanosine nucleotides. -!- An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. -!- The enzyme can catalyze the second reaction alone in the presence of ammonia. -!- Formerly EC 6.3.4.1. P49433 P49433 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. P49814 P49814 1.1.1.37 Malate dehydrogenase. Malic dehydrogenase. (S)-malate + NAD(+) = oxaloacetate + NADH. -!- Also oxidizes some other 2-hydroxydicarboxylic acids. P50308 P50308 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P50620 P50620 1.17.4.1 Ribonucleoside-diphosphate reductase. Ribonucleotide reductase. 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Fe(3+) or adenosylcob(III)alamin or Mn(2+). -!- This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. -!- There are three types of this enzyme differing in their cofactors. -!- Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. -!- In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6 and EC 1.17.4.2. P50735 P50735 1.4.1.2 Glutamate dehydrogenase. Glutamic dehydrogenase. L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH. P50831 P50831 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P50848 P50848 3.4.17.19 Carboxypeptidase Taq. Carboxypeptidase 1. Release of a C-terminal amino acid with broad specificity, except for -Pro. Zn(2+). -!- Most active at 80 degrees Celsius. -!- Belongs to peptidase family M32. P50849 P50849 2.7.7.8 Polyribonucleotide nucleotidyltransferase. Polynucleotide phosphorylase. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. -!- ADP, IDP, GDP, UDP and CDP can act as donors. P51831 P51831 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH. -!- Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates. P51833 P51833 3.1.26.3 Ribonuclease III. Ribonuclease 3. RNase III. Endonucleolytic cleavage to 5'-phosphomonoester. -!- An endoribonuclease that cleaves double-stranded RNA molecules. -!- The cleavage can be either a single-stranded nick or double-stranded break in the RNA, depending in part upon the degree of base-pairing in the region of the cleavage site. -!- Specificity is conferred by negative determinants, i.e., the presence of certain Watson-Crick base-pairs at specific positions that strongly inhibit cleavage. -!- RNase III is involved in both rRNA processing and mRNA processing and decay. P52042 P52042 1.3.8.1 Short-chain acyl-CoA dehydrogenase. Butanoyl-CoA dehydrogenase. Butyryl dehydrogenase. Short-chain acyl CoA dehydrogenase. Unsaturated acyl-CoA reductase. A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein. FAD. -!- One of several enzymes that catalyze the first step in fatty acids beta-oxidation. -!- The enzyme catalyzes the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R hydrogen atoms. -!- The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. -!- The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA. -!- The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA. -!- Cf. EC 1.3.8.7, EC 1.3.8.8 and EC 1.3.8.9. -!- Formerly EC 1.3.2.1 and EC 1.3.99.2. P52046 P52046 4.2.1.150 Short-chain-enoyl-CoA hydratase. 3-hydroxybutyryl-CoA dehydratase. Crotonase. A short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2-enoyl-CoA + H(2)O. -!- The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents. -!- It is specific for short, C(4)-C(6), chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA. -!- Cf. EC 4.2.1.17 and EC 4.2.1.74. P52208 P52208 1.1.1.44 Phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating). 6-phosphogluconic carboxylase. 6-phosphogluconic dehydrogenase. 6PGD. Phosphogluconic acid dehydrogenase. 6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH. -!- The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. -!- Highly specific for NADP(+). -!- Cf. EC 1.1.1.343. P52415 P52415 2.7.7.27 Glucose-1-phosphate adenylyltransferase. ADP-glucose diphosphorylase. ADP-glucose pyrophosphorylase. ADP-glucose synthase. ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose. P52697 P52697 3.1.1.31 6-phosphogluconolactonase. 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-phospho-D-gluconate. P52983 P52983 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. P53593 P53593 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P54205 P54205 4.1.1.39 Ribulose-bisphosphate carboxylase. Carboxydismutase. D-ribulose 1,5-diphosphate carboxylase. D-ribulose-1,5-bisphosphate carboxylase. Diphosphoribulose carboxylase. Ribulose 1,5-bisphosphate carboxylase. Ribulose 1,5-bisphosphate carboxylase/oxygenase. Ribulose 1,5-diphosphate carboxylase. Ribulose 1,5-diphosphate carboxylase/oxygenase. Ribulose bisphosphate carboxylase/oxygenase. Ribulose diphosphate carboxylase. Ribulose diphosphate carboxylase/oxygenase. RuBisCO. RuBP carboxylase. 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O. -!- Will utilize O(2) instead of CO(2), forming 3-phospho-D-glycerate and 2-phosphoglycolate. P54206 P54206 4.1.1.39 Ribulose-bisphosphate carboxylase. Carboxydismutase. D-ribulose 1,5-diphosphate carboxylase. D-ribulose-1,5-bisphosphate carboxylase. Diphosphoribulose carboxylase. Ribulose 1,5-bisphosphate carboxylase. Ribulose 1,5-bisphosphate carboxylase/oxygenase. Ribulose 1,5-diphosphate carboxylase. Ribulose 1,5-diphosphate carboxylase/oxygenase. Ribulose bisphosphate carboxylase/oxygenase. Ribulose diphosphate carboxylase. Ribulose diphosphate carboxylase/oxygenase. RuBisCO. RuBP carboxylase. 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O. -!- Will utilize O(2) instead of CO(2), forming 3-phospho-D-glycerate and 2-phosphoglycolate. P54224 P54224 4.1.1.37 Uroporphyrinogen decarboxylase. Uroporphyrinogen III decarboxylase. Uroporphyrinogen-III carboxy-lyase. Uroporphyrinogen III = coproporphyrinogen + 4 CO(2). -!- Acts on a number of porphyrinogens. P54375 P54375 1.15.1.1 Superoxide dismutase. 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Fe cation or Mn(2+) or (Zn(2+) and Cu cation). P54376 P54376 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. P54380 P54380 6.1.1.14 Glycine--tRNA ligase. Glycyl translase. Glycyl-tRNA synthetase. ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). P54418 P54418 4.1.1.49 Phosphoenolpyruvate carboxykinase (ATP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2). P54419 P54419 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. P54470 P54470 2.7.4.27 ([Pyruvate, phosphate dikinase] phosphate) phosphotransferase. Bifunctional dikinase regulatory protein. PPDK regulatory protein. Pyruvate, phosphate dikinase regulatory protein. [Pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate. -!- The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyzes the phosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.11.32. -!- Formerly EC 2.7.4.n1. P54470 P54470 2.7.11.32 [Pyruvate, phosphate dikinase] kinase. Bifunctional dikinase regulatory protein. PPDK regulatory protein. Pyruvate, phosphate dikinase regulatory protein. ADP + [pyruvate, phosphate dikinase] = AMP + [pyruvate, phosphate dikinase] phosphate. -!- The enzyme from the plants Zea mays (maize) and Arabidopsis is bifunctional and catalyzes both the phosphorylation and dephosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.4.27. -!- The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates an active site histidine. -!- Formerly EC 2.7.11.n1. P54471 P54471 2.1.1.217 tRNA (adenine(22)-N(1))-methyltransferase. S-adenosyl-L-methionine + adenine(22) in tRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(22) in tRNA. -!- The enzyme specifically methylates adenine(22) in tRNA. -!- Formerly EC 2.1.1.36. P54517 P54517 4.2.1.10 3-dehydroquinate dehydratase. 3-dehydroquinate = 3-dehydroshikimate + H(2)O. P54523 P54523 2.2.1.7 1-deoxy-D-xylulose-5-phosphate synthase. 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating). 1-deoxyxylulose-5-phosphate synthase. DXP-synthase. Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO(2). Thiamine diphosphate. -!- The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. -!- Formerly EC 4.1.3.37. P54530 P54530 2.3.1.19 Phosphate butyryltransferase. Phosphotransbutyrylase. Butanoyl-CoA + phosphate = CoA + butanoylphosphate. P54555 P54555 4.3.1.18 D-serine ammonia-lyase. D-hydroxy amino acid dehydratase. D-serine deaminase. D-serine dehydrase. D-serine dehydratase. D-serine dehydratase (deaminating). D-serine hydro-lyase (deaminating). D-serine hydrolase. D-serine = pyruvate + NH(3). Pyridoxal 5'-phosphate. -!- The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- Also acts, slowly, on D-threonine. -!- Formerly EC 4.2.1.14. P54616 P54616 1.3.1.9 Enoyl-[acyl-carrier-protein] reductase (NADH). Enoyl-ACP reductase. NADH-enoyl acyl carrier protein reductase. NADH-specific enoyl-ACP reductase. An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH. -!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons. P54691 P54691 2.6.1.42 Branched-chain-amino-acid transaminase. Branched-chain amino acid aminotransferase. Transaminase B. L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. Pyridoxal 5'-phosphate. -!- Also acts on L-isoleucine and L-valine. -!- Different from EC 2.6.1.66. P54735 P54735 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P54741 P54741 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P55038 P55038 1.4.7.1 Glutamate synthase (ferredoxin). Ferredoxin-dependent glutamate synthase. 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H(+). FAD; FMN; Iron-sulfur. -!- The protein is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate. -!- The NH(3) is channeled through a 24 A channel in the active protein. -!- No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein. P55989 P55989 7.2.2.9 P-type Cu(2+) transporter. Cu(2+)-exporting ATPase. ATP + H(2)O + Cu(2+)(Side 1) = ADP + phosphate + Cu(2+)(Side 2). Mg(2+). -!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- The enzyme from the termophilic bacterium Archaeoglobus fulgidus is involved in copper extrusion from the cell. -!- Formerly EC 3.6.3.4. P55992 P55992 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P56069 P56069 2.5.1.48 Cystathionine gamma-synthase. Cystathionine synthase. Cystathionine synthetase. Homoserine O-transsuccinylase. Homoserine transsuccinylase. O-succinyl-L-homoserine succinate-lyase (adding cysteine). O-succinylhomoserine (thiol)-lyase. O-succinylhomoserine synthase. O-succinylhomoserine synthetase. O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate. Pyridoxal 5'-phosphate. -!- Also reacts with H(2)S and methanethiol as replacing agents, producing homocysteine and methionine, respectively. -!- In the absence of thiol, can also catalyze beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia. -!- Formerly EC 4.2.99.9. P56119 P56119 1.1.1.25 Shikimate dehydrogenase. 5-dehydroshikimate reductase. 5-dehydroshikimic reductase. Dehydroshikimic reductase. DHS reductase. Shikimate 5-dehydrogenase. Shikimate oxidoreductase. Shikimate:NADP(+) 5-oxidoreductase. Shikimate:NADP(+) oxidoreductase. Shikimate + NADP(+) = 3-dehydroshikimate + NADPH. -!- NAD(+) cannot replace NADP(+). -!- In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10. P56123 P56123 3.1.13.1 Exoribonuclease II. Ribonuclease II. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. -!- Preference for single-stranded RNA. -!- The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5. -!- Similar enzymes: RNase Q, RNase BN, RNase PIII, RNase Y. -!- Formerly EC 3.1.4.20. P56197 P56197 2.5.1.19 3-phosphoshikimate 1-carboxyvinyltransferase. 3-enol-pyruvoylshikimate-5-phosphate synthase. 5-enolpyruvylshikimate-3-phosphate synthase. EPSP synthase. Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate. P56258 P56258 2.4.1.325 TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase. dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose + N-acetyl-beta-D- mannosaminouronyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho- ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-alpha-D- galactosyl-(1->4)-N-acetyl-beta-D-mannosaminouronyl-(1->4)-N-acetyl- alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol. -!- Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. -!- The trisaccharide of the product (lipid III) is the repeat unit of ECA. P57698 P57698 7.2.2.6 P-type K(+) transporter. K(+)-importing ATPase. K(+)-transporting ATPase. Potassium-importing ATPase. ATP + H(2)O + K(+)(Side 1) = ADP + phosphate + K(+)(Side 2). Mg(2+). -!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- A bacterial enzyme that is involved in K(+) import. -!- The probable stoichiometry is one ion per ATP hydrolyzed. -!- Formerly EC 3.6.3.12. P58130 P58130 2.3.1.15 Glycerol-3-phosphate 1-O-acyltransferase. Glycerol-3-phosphate O-acyltransferase. Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. -!- Acyl-[acyl-carrier-protein] can also act as acyl donor. -!- Acts only with derivatives of fatty acids of chain length above C(10). P58176 P58176 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). P58255 P58255 2.3.1.19 Phosphate butyryltransferase. Phosphotransbutyrylase. Butanoyl-CoA + phosphate = CoA + butanoylphosphate. P58262 P58262 2.8.1.10 Thiazole synthase. 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur- carrier protein ThiS] = 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- ylidene)ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H(2)O. -!- H(2)S can provide the sulfur in vitro. -!- Part of the pathway for thiamine biosynthesis. P58363 P58363 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P58473 P58473 3.4.11.23 PepB aminopeptidase. Aminopeptidase B. Peptidase B. Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln. -!- A 270-kDa protein composed of six 46.3-kDa subunits. -!- The pH optimum is in the alkaline range and activity is stimulated by KCl. -!- Belongs to peptidase family M17. P58694 P58694 6.1.1.22 Asparagine--tRNA ligase. Asparagine translase. Asparaginyl-tRNA synthetase. ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl- tRNA(Asn). P59107 P59107 3.1.13.1 Exoribonuclease II. Ribonuclease II. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. -!- Preference for single-stranded RNA. -!- The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5. -!- Similar enzymes: RNase Q, RNase BN, RNase PIII, RNase Y. -!- Formerly EC 3.1.4.20. P59393 P59393 2.7.9.3 Selenide, water dikinase. Selenide,water dikinase. Selenium donor protein. Selenophosphate synthase. Selenophosphate synthetase. ATP + selenide + H(2)O = AMP + selenophosphate + phosphate. Mg(2+). P59395 P59395 4.2.1.149 Crotonobetainyl-CoA hydratase. L-carnityl-CoA dehydratase. L-carnitinyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA + H(2)O. -!- The enzyme is also able to use crotonyl-CoA as substrate, with low efficiency. -!- Formerly EC 4.2.1.89. P59409 P59409 1.1.1.103 L-threonine 3-dehydrogenase. TDH. L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH. -!- Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine. -!- This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex. -!- In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone. P59600 P59600 3.5.1.16 Acetylornithine deacetylase. Acetylornithinase. N-acetylornithinase. N(2)-acetyl-L-ornithine + H(2)O = acetate + L-ornithine. -!- Also hydrolyzes N-acetylmethionine. P59609 P59609 6.3.4.5 Argininosuccinate synthase. Arginine succinate synthetase. Argininosuccinate synthetase. Citrulline--aspartate ligase. ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate. P59740 P59740 2.7.7.4 Sulfate adenylyltransferase. ATP-sulfurylase. Sulfate adenylate transferase. Sulfurylase. ATP + sulfate = diphosphate + adenylyl sulfate. -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. P59746 P59746 3.5.1.105 Chitin disaccharide deacetylase. Chitin oligosaccharide amidohydolase. Chitin oligosaccharide deacetylase. Chitobiose amidohydolase. N,N'-diacetylchitobiose + H(2)O = N-acetyl-beta-D-glucosaminyl-(1->4)-D- glucosamine + acetate. -!- Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. -!- Besides being a nutrient, the heterodisaccharide product 4-O- (N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus. -!- In contrast to EC 3.5.1.41 this enzyme is specific for the chitin disaccharide. -!- It also deacetylates the chitin trisaccharide with lower efficiency. -!- No activity with higher polymers of GlcNAc. P60546 P60546 2.7.4.8 Guanylate kinase. Deoxyguanylate kinase. GMP kinase. Guanosine monophosphate kinase. ATP + GMP = ADP + GDP. -!- dGMP can also act as acceptor. -!- dATP can act as donor. P60651 P60651 3.5.3.11 Agmatinase. Agmatine ureohydrolase. Agmatine + H(2)O = putrescine + urea. P60718 P60718 2.8.1.8 Lipoyl synthase. Lipoate synthase. [Protein]-N(6)-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S](2+) cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H(+) = [protein]-N(6)-((R)-dihydrolipoyl)-L- lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe(3+) + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin. Iron-sulfur. -!- This enzyme catalyzes the final step in the de novo biosynthesis of the lipoyl cofactor, the attachment of two sulfhydryl groups to C(6) and C(8) of a pendant octanoyl chain. -!- It is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (S-adenosylmethionine) by the addition of an electron from an iron-sulfur center. -!- The enzyme contains two [4Fe-4S] clusters. -!- The first cluster produces the radicals, which are converted into 5'-deoxyadenosine when they abstract hydrogen atoms from C(6) and C(8), respectively, leaving reactive radicals at these positions that interact with sulfur atoms within the second (auxiliary) cluster. -!- Having donated two sulfur atoms, the auxiliary cluster is degraded during catalysis, but is regenerated immediately by the transfer of a new cluster from iron-sulfur cluster carrier proteins. -!- Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. -!- Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). -!- An alternative lipoylation pathway involves EC 6.3.1.20, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs). P60752 P60752 7.5.2.6 ABC-type lipid A-core oligosaccharide transporter. ATP-dependent lipid A-core flippase. Lipid flippase. ATP + H(2)O + lipid A-core oligosaccharide(Side 1) = ADP + phosphate + lipid A-core oligosaccharide(Side 2). -!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- The enzyme, best characterized from the bacterium Escherichia coli, is located in the inner membrane and mediates the movement of lipid A attached to the core oligosaccharide from the cytoplasm to the periplasmic side of the inner membrane, an important step in the lipopolysaccharide biosynthetic pathway. -!- Not to be confused with EC 7.5.2.5, which is implicated in the translocation of LPS from the inner membrane to the outer membrane and acts later in the process. P60788 P60788 3.6.5.n1 Elongation factor 4. GTP + H(2)O = GDP + phosphate. -!- The enzyme is required for accurate and efficient protein synthesis under certain stress conditions. -!- May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. -!- Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. -!- Binds to ribosomes in a GTP-dependent manner. P60908 P60908 6.1.1.21 Histidine--tRNA ligase. Histidine translase. Histidyl-tRNA synthetase. ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). P60929 P60929 2.3.1.275 Acyl phosphate:glycerol-3-phosphate acyltransferase. Acyl-phosphate--glycerol-3-phosphate acyltransferase. Acyl-PO(4) G3P acyltransferase. G3P acyltransferase. Glycerol-3-phosphate acyltransferase (acyl-phosphate transferring). GPAT. LPA synthase. Lysophosphatidic acid synthase. An acyl-phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycerol 3-phosphate + phosphate. -!- The enzyme, found in bacteria, catalyzes a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. -!- The enzyme is membrane-bound. -!- Formerly EC 2.3.1.n3. P61488 P61488 2.7.2.4 Aspartate kinase. Aspartokinase. ATP + L-aspartate = ADP + 4-phospho-L-aspartate. -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3. -!- This is also the case for two of the four isoenzymes in Arabidopsis thaliana. -!- The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction. P61517 P61517 4.2.1.1 Carbonic anhydrase. Carbonate dehydratase. Carbonate hydro-lyase. Carbonic dehydratase. H(2)CO(3) = CO(2) + H(2)O. Zn(2+). -!- The enzyme catalyzes the reversible hydration of gaseous CO(2) to carbonic acid, which spontaneously converts to hydrogencarbonate under neutral pH. -!- It is widespread and found in archaea, bacteria, and eukaryotes. -!- Three distinct classes exist, and appear to have evolved independently. P61518 P61518 4.2.1.1 Carbonic anhydrase. Carbonate dehydratase. Carbonate hydro-lyase. Carbonic dehydratase. H(2)CO(3) = CO(2) + H(2)O. Zn(2+). -!- The enzyme catalyzes the reversible hydration of gaseous CO(2) to carbonic acid, which spontaneously converts to hydrogencarbonate under neutral pH. -!- It is widespread and found in archaea, bacteria, and eukaryotes. -!- Three distinct classes exist, and appear to have evolved independently. P61887 P61887 2.7.7.24 Glucose-1-phosphate thymidylyltransferase. dTDP-glucose diphosphorylase. dTDP-glucose pyrophosphorylase. dTDP-glucose synthase. dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose. P61889 P61889 1.1.1.37 Malate dehydrogenase. Malic dehydrogenase. (S)-malate + NAD(+) = oxaloacetate + NADH. -!- Also oxidizes some other 2-hydroxydicarboxylic acids. P62622 P62622 1.17.7.3 (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin). (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase. (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H(2)O + oxidized flavodoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin. -!- Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria. -!- Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1). P62707 P62707 5.4.2.11 Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). 2,3-diphosphoglycerate dependent phosphoglycerate mutase. Cofactor dependent phosphoglycerate mutase. PGAM. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. -!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. P62709 P62709 5.4.2.11 Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). 2,3-diphosphoglycerate dependent phosphoglycerate mutase. Cofactor dependent phosphoglycerate mutase. PGAM. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. -!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. P62710 P62710 5.4.2.11 Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). 2,3-diphosphoglycerate dependent phosphoglycerate mutase. Cofactor dependent phosphoglycerate mutase. PGAM. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. -!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. P63180 P63180 2.1.1.185 23S rRNA (guanosine(2251)-2'-O)-methyltransferase. S-adenosyl-L-methionine + guanosine(2251) in 23S rRNA = S-adenosyl-L- homocysteine + 2'-O-methylguanosine(2251) in 23S rRNA. -!- The enzyme catalyzes the methylation of guanosine(2251), a modification conserved in the peptidyltransferase domain of 23S rRNA. P63224 P63224 5.3.1.28 D-sedoheptulose 7-phosphate isomerase. Phosphoheptose isomerase. Sedoheptulose-7-phosphate isomerase. D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. -!- In Gram-negative bacteria the enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core. -!- In Gram-positive bacteria the enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein. P63610 P63610 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. P63634 P63634 5.1.1.3 Glutamate racemase. L-glutamate = D-glutamate. Pyridoxal 5'-phosphate. P63737 P63737 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. P64074 P64074 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. P64149 P64149 3.2.2.23 DNA-formamidopyrimidine glycosylase. Fapy-DNA glycosylase. Formamidopyrimidine-DNA glycosylase. Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. -!- May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. -!- Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA. P64149 P64149 4.2.99.18 DNA-(apurinic or apyrimidinic site) lyase. AP endonuclease class I. AP lyase. Deoxyribonuclease (apurinic or apyrimidinic). E.coli endonuclease III. Endodeoxyribonuclease (apurinic or apyrimidinic). Micrococcus luteus UV endonuclease. Phage-T(4) UV endonuclease. Phage-T4 UV endonuclease. The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. -!- 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. -!- This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2. P64258 P64258 2.7.8.13 Phospho-N-acetylmuramoyl-pentapeptide-transferase. MraY transferase. Phospho-MurNAc-pentapeptide transferase. Phospho-N-acetylmuramoyl pentapeptide translocase. Phospho-NAc-muramoyl-pentapeptide translocase (UMP). Phosphoacetylmuramoylpentapeptide translocase. Phosphoacetylmuramoylpentapeptidetransferase. UDP-MurNAc-Ala-gamma-DGlu-Lys-DAla-DAla:undecaprenylphosphate transferase. UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C(55)-isoprenoid alcohol transferase. UDP-MurNAc-pentapeptide phosphotransferase. UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- diphosphoundecaprenol. -!- In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-center. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. P65330 P65330 4.4.1.21 S-ribosylhomocysteine lyase. S-ribosylhomocysteinase. S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5- dihydroxypentan-2,3-dione. Fe(2+). -!- The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density. -!- Formerly EC 3.2.1.148 and EC 3.3.1.3. P66699 P66699 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P66794 P66794 2.7.9.3 Selenide, water dikinase. Selenide,water dikinase. Selenium donor protein. Selenophosphate synthase. Selenophosphate synthetase. ATP + selenide + H(2)O = AMP + selenophosphate + phosphate. Mg(2+). P67911 P67911 5.1.3.20 ADP-glyceromanno-heptose 6-epimerase. ADP-L-glycero-D-manno-heptose 6-epimerase. ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose. NAD(+). P68187 P68187 7.5.2.1 ABC-type maltose transporter. Maltose-transporting ATPase. ATP + H(2)O + maltose-[maltose-binding protein](Side 1) = ADP + phosphate + maltose(Side 2) + [maltose-binding protein](Side 1). -!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of maltose and maltose oligosaccharides. -!- Formerly EC 3.6.3.19. P68567 P68567 2.1.1.242 16S rRNA (guanine(1516)-N(2))-methyltransferase. M(2)G(1516) methyltransferase. S-adenosyl-L-methionine + guanine(1516) in 16S rRNA = S-adenosyl-L- homocysteine + N(2)-methylguanine(1516) in 16S rRNA. -!- The enzyme specifically methylates guanine(1516) at N(2) in 16S rRNA. P69441 P69441 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. P69503 P69503 2.4.2.7 Adenine phosphoribosyltransferase. AMP diphosphorylase. AMP pyrophosphorylase. APRT. Transphosphoribosidase. AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. -!- 5-amino-4-imidazolecarboxamide can replace adenine. P69786 P69786 2.7.1.199 Protein-N(pi)-phosphohistidine--D-glucose phosphotransferase. D-glucose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-glucose(Side 1) = [protein]-L- histidine + D-glucose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P69795 P69795 2.7.1.196 Protein-N(pi)-phosphohistidine--N,N'-diacetylchitobiose phosphotransferase. Chitobiose PTS permease. N,N'-diacetylchitobiose PTS permease. [Protein]-N(pi)-phospho-L-histidine + N,N'-diacetylchitobiose(Side 1) = [protein]-L-histidine + N,N'-diacetylchitobiose 6'-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P69797 P69797 2.7.1.191 Protein-N(pi)-phosphohistidine--D-mannose phosphotransferase. Mannose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L- histidine + D-mannose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P69799 P69799 2.7.1.191 Protein-N(pi)-phosphohistidine--D-mannose phosphotransferase. Mannose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L- histidine + D-mannose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P69908 P69908 4.1.1.15 Glutamate decarboxylase. L-glutamate 1-carboxy-lyase. L-glutamate = 4-aminobutanoate + CO(2). Pyridoxal 5'-phosphate. -!- The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. P69910 P69910 4.1.1.15 Glutamate decarboxylase. L-glutamate 1-carboxy-lyase. L-glutamate = 4-aminobutanoate + CO(2). Pyridoxal 5'-phosphate. -!- The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. P69911 P69911 4.1.1.15 Glutamate decarboxylase. L-glutamate 1-carboxy-lyase. L-glutamate = 4-aminobutanoate + CO(2). Pyridoxal 5'-phosphate. -!- The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. P69923 P69923 5.3.1.25 L-fucose isomerase. L-fucopyranose = L-fuculose. Mn(2+). -!- The enzyme binds the closed form of the sugar and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene- diol mechanism. -!- The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose. -!- The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose. P69925 P69925 1.17.4.1 Ribonucleoside-diphosphate reductase. Ribonucleotide reductase. 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Fe(3+) or adenosylcob(III)alamin or Mn(2+). -!- This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. -!- There are three types of this enzyme differing in their cofactors. -!- Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. -!- In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6 and EC 1.17.4.2. P71012 P71012 2.7.1.202 Protein-N(pi)-phosphohistidine--D-fructose phosphotransferase. Fructose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-fructose(Side 1) = [protein]-L- histidine + D-fructose 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P71035 P71035 3.5.1.5 Urease. Urea + H(2)O = CO(2) + 2 NH(3). Ni(2+). P71051 P71051 2.7.10.2 Non-specific protein-tyrosine kinase. Cytoplasmic protein tyrosine kinase. ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. -!- Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain. -!- In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families. -!- Formerly EC 2.7.1.112. P71104 P71104 2.7.2.1 Acetate kinase. Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK. ATP + acetate = ADP + acetyl phosphate. Mg(2+). -!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. P71447 P71447 5.4.2.6 Beta-phosphoglucomutase. Beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate. -!- The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate. -!- Although this is a slow reaction, only a single turnover is required for activation. -!- Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles. -!- Cf. EC 5.4.2.2. P71707 P71707 2.4.1.129 Peptidoglycan glycosyltransferase. Bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)- pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D- glucosaminyltransferase. Penicillin binding protein (3 or 1B). Peptidoglycan TGase. Peptidoglycan transglycosylase. PG-II. (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)- diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala- gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate. -!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. -!- Involved in the synthesis of cell-wall peptidoglycan. P71707 P71707 3.4.16.4 Serine-type D-Ala-D-Ala carboxypeptidase. D-alanyl-D-alanine carboxypeptidase. DD-peptidase. DD-transpeptidase. Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. -!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13. P71741 P71741 3.2.1.28 Alpha,alpha-trehalase. Trehalase. Alpha,alpha-trehalose + H(2)O = beta-D-glucose + alpha-D-glucose. -!- The enzyme is an anomer-inverting glucosidase that catalyzes the hydrolysis of the alpha-glucosidic O-linkage of alpha,alpha- trehalose, releasing initially equimolar amounts of alpha- and beta- D-glucose. -!- It is widely distributed in microorganisms, plants, invertebrates and vertebrates. P72584 P72584 1.14.13.81 Magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase. Mg-protoporphyrin IX monomethyl ester oxidative cyclase. Magnesium-protoporphyrin IX 13-monomethyl ester + 3 NADPH + 3 O(2) = 3,8- divinyl protochlorophyllide + 3 NADP(+) + 5 H(2)O. Fe cation. -!- The enzyme participates in the biosynthesis of chlorophyllide a in aerobic organisms. -!- The same transformation is achieved in anaerobic organisms by EC 1.21.98.3. -!- Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes. P72641 P72641 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. P72648 P72648 2.7.4.8 Guanylate kinase. Deoxyguanylate kinase. GMP kinase. Guanosine monophosphate kinase. ATP + GMP = ADP + GDP. -!- dGMP can also act as acceptor. -!- dATP can act as donor. P72659 P72659 2.7.7.8 Polyribonucleotide nucleotidyltransferase. Polynucleotide phosphorylase. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. -!- ADP, IDP, GDP, UDP and CDP can act as donors. P72797 P72797 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. P72849 P72849 1.14.14.18 Heme oxygenase (biliverdin-producing). Heme oxidase. Heme oxygenase. Heme oxygenase (decyclizing). Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O. -!- This mammalian enzyme participates in the degradation of heme. -!- The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. -!- The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. -!- The enzyme requires NAD(P)H and EC 1.6.2.4. -!- Cf. EC 1.14.15.20. -!- Formerly EC 1.14.99.3. P72854 P72854 1.8.7.1 Assimilatory sulfite reductase (ferredoxin). Sulfite reductase (ferredoxin). Hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H(2)O = sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H(+). Fe cation. -!- The enzyme participates in sulfate assimilation. -!- While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria (cf. EC 1.8.1.2). -!- Formerly EC 1.8.99.1. P72871 P72871 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. P72940 P72940 2.7.1.25 Adenylyl-sulfate kinase. Adenosine 5'-phosphosulfate kinase. Adenylylsulfate kinase. APS kinase. ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate. -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. P72965 P72965 2.5.1.3 Thiamine phosphate synthase. Thiamine-phosphate diphosphorylase. Thiamine-phosphate pyrophosphorylase. Thiamine-phosphate synthase. TMP diphosphorylase. TMP pyrophosphorylase. (1) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy- 4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (2) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4- methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (3) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5- (2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. -!- The enzyme catalyzes the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. -!- The enzyme is thought to accept the product of EC 2.8.1.10 as its substrate. -!- However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, EC 5.3.99.10 converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. -!- In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products. -!- In yeast this activity is found in a bifunctional enzyme and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme. P73053 P73053 2.1.1.148 Thymidylate synthase (FAD). FDTS. Flavin dependent thymidylate synthase. 5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+). -!- Contains FAD. -!- All thymidylate synthases catalyze a reductive methylation involving the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5-position of dUMP and a two electron reduction of the methylene group to a methyl group. -!- Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses folate as both a 1-carbon donor and a source of reducing equivalents, this enzyme uses a flavin coenzyme as a source of reducing equivalents, which are derived from NADPH. P73067 P73067 2.2.1.7 1-deoxy-D-xylulose-5-phosphate synthase. 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating). 1-deoxyxylulose-5-phosphate synthase. DXP-synthase. Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO(2). Thiamine diphosphate. -!- The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. -!- Formerly EC 4.1.3.37. P73127 P73127 2.8.4.3 tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase. 2-methylthio-N-6-isopentenyl adenosine synthase. tRNA-i6A37 methylthiotransferase. N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio- N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor. Iron-sulfur. -!- This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur. -!- The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes. -!- The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. -!- The identity of the electron donor is not known. P73257 P73257 4.3.2.1 Argininosuccinate lyase. Arginosuccinase. N-(L-argininosuccinate) arginine-lyase. Omega-N-(L-arginino)succinate arginine-lyase. 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. P73274 P73274 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). P73290 P73290 6.3.4.4 Adenylosuccinate synthase. Adenylosuccinate synthetase. IMP--aspartate ligase. Succinoadenylic kinosynthetase. GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)- AMP. P73334 P73334 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P73411 P73411 1.1.1.49 Glucose-6-phosphate dehydrogenase (NADP(+)). G6PD. G6PDH. Glucose-6-phosphate 1-dehydrogenase. Glucose-6-phosphate dehydrogenase. GPD. D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + NADPH. -!- The enzyme catalyzes a step of the pentose phosphate pathway. -!- The enzyme is specific for NADP(+), cf. EC 1.1.1.363 and EC 1.1.1.388. P73469 P73469 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P73505 P73505 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). P73534 P73534 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). P73617 P73617 2.4.2.18 Anthranilate phosphoribosyltransferase. Phosphoribosyl-anthranilate diphosphorylase. Phosphoribosyl-anthranilate pyrophosphorylase. N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate. -!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20 and EC 5.3.1.24). P73632 P73632 6.3.2.4 D-alanine--D-alanine ligase. Alanine:alanine ligase (ADP-forming). Alanylalanine synthetase. D-Ala-D-Ala synthetase. D-alanyl-D-alanine synthetase. D-alanylalanine synthetase. ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. -!- Involved with EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide. P73648 P73648 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. P73728 P73728 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P73755 P73755 2.8.1.13 tRNA-uridine 2-sulfurtransferase. A [protein]-S-sulfanyl-L-cysteine + uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + acceptor. -!- The enzyme, found in bacteria, catalyzes formation of the 2-thiouridine modification in the wobble position of tRNA(Gln), tRNA(Lys) and tRNA(Glu). P73810 P73810 5.6.2.2 DNA topoisomerase. DNA topoisomerase I. Nicking-closing enzyme. Omega-protein. Relaxing enzyme. Swivelase. Type I DNA topoisomerase. Untwisting enzyme. ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. -!- These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.6.2.3. -!- Formerly EC 5.99.1.2. P73821 P73821 1.1.1.95 Phosphoglycerate dehydrogenase. 3-phosphoglycerate dehydrogenase. 3-phosphoglyceric acid dehydrogenase. 3PHP reductase. Alpha-KG reductase. Alpha-phosphoglycerate dehydrogenase. D-3-phosphoglycerate dehydrogenase. Glycerate 3-phosphate dehydrogenase. Glycerate-1,3-phosphate dehydrogenase. PGDH. Phosphoglycerate oxidoreductase. Phosphoglyceric acid dehydrogenase. 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. -!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399. P73821 P73821 1.1.1.399 2-oxoglutarate reductase. (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. -!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95. P73824 P73824 1.11.1.22 Hydroperoxy fatty acid reductase. A hydroperoxy fatty acid + NADPH = a hydroxy fatty acid + NADP(+) + H(2)O. -!- The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. -!- The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation. P73826 P73826 1.1.1.36 Acetoacetyl-CoA reductase. (R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-CoA + NADPH. P73833 P73833 6.3.2.29 Cyanophycin synthase (L-aspartate-adding). Cyanophycin synthetase. Multi-L-arginyl-poly-L-aspartate synthase. ATP + (L-Asp(4-L-Arg))(n) + L-Asp = ADP + phosphate + (L-Asp(4-L- Arg))(n)-L-Asp. Mg(2+). -!- Both this enzyme and EC 6.3.2.30 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store. -!- Both enzymes are found in the same protein but have different active sites. -!- Both L-Asp and L-Arg must be present before either enzyme will display significant activity. P73833 P73833 6.3.2.30 Cyanophycin synthase (L-arginine-adding). Cyanophycin synthetase. Multi-L-arginyl-poly-L-aspartate synthase. ATP + (L-Asp(4-L-Arg))(n)-L-Asp + L-Arg = ADP + phosphate + (L-Asp(4-L- Arg))(n+1). Mg(2+). -!- Both this enzyme and EC 6.3.2.29 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store. -!- Both enzymes are found in the same protein but have different active sites. -!- Both L-Asp and L-Arg must be present before either enzyme will display significant activity. -!- Canavanine and lysine can be incoporated into the polymer instead of arginine. P73849 P73849 3.1.3.71 2-phosphosulfolactate phosphatase. (2R)-phosphosulfolactate phosphohydrolase. ComB phosphatase. (2R)-2-phospho-3-sulfolactate + H(2)O = (2R)-3-sulfolactate + phosphate. Mg(2+). -!- The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyzes a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. -!- This enzyme can also hydrolyze phosphate monoesters of (R)-2- hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)- 2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations. P73867 P73867 7.2.2.6 P-type K(+) transporter. K(+)-importing ATPase. K(+)-transporting ATPase. Potassium-importing ATPase. ATP + H(2)O + K(+)(Side 1) = ADP + phosphate + K(+)(Side 2). Mg(2+). -!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- A bacterial enzyme that is involved in K(+) import. -!- The probable stoichiometry is one ion per ATP hydrolyzed. -!- Formerly EC 3.6.3.12. P73922 P73922 3.1.3.11 Fructose-bisphosphatase. Fructose 1,6-bisphosphatase. Hexose diphosphatase. D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. -!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. P73922 P73922 3.1.3.37 Sedoheptulose-bisphosphatase. Sedoheptulose-1,7-bisphosphatase. Sedoheptulose 1,7-bisphosphate + H(2)O = sedoheptulose 7-phosphate + phosphate. P73933 P73933 2.3.1.275 Acyl phosphate:glycerol-3-phosphate acyltransferase. Acyl-phosphate--glycerol-3-phosphate acyltransferase. Acyl-PO(4) G3P acyltransferase. G3P acyltransferase. Glycerol-3-phosphate acyltransferase (acyl-phosphate transferring). GPAT. LPA synthase. Lysophosphatidic acid synthase. An acyl-phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycerol 3-phosphate + phosphate. -!- The enzyme, found in bacteria, catalyzes a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. -!- The enzyme is membrane-bound. -!- Formerly EC 2.3.1.n3. P73960 P73960 1.1.1.85 3-isopropylmalate dehydrogenase. Beta-IPM dehydrogenase. Beta-isopropylmalate dehydrogenase. IMDH. (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH. P74007 P74007 3.1.7.2 Guanosine-3',5'-bis(diphosphate) 3'-diphosphatase. (ppGpp)ase. Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase. Penta-phosphate guanosine-3'-diphosphohydrolase. Penta-phosphate guanosine-3'-pyrophosphohydrolase. Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate. P74106 P74106 4.3.2.10 Imidazole glycerol-phosphate synthase. IGP synthase. 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho- beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1- (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1- (imidazol-4-yl)glycerol 3-phosphate + L-glutamate. -!- The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. -!- The enzymes from archaea and bacteria are heterodimeric. -!- A glutaminase component (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. -!- The glutminase subunit is only active within the dimeric complex. -!- In fungi and plants the two subunits are combined into a single polypeptide. P74122 P74122 2.3.1.1 Amino-acid N-acetyltransferase. N-acetylglutamate synthase. Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. -!- Also acts with L-aspartate and, more slowly, with some other amino acids. P74122 P74122 2.3.1.35 Glutamate N-acetyltransferase. Acetylglutamate synthetase. Acetylglutamate-acetylornithine transacetylase. Acetylglutamic synthetase. Acetylglutamic-acetylornithine transacetylase. Acetylornithinase. Acetylornithine glutamate acetyltransferase. Glutamate acetyltransferase. N-acetyl-L-glutamate synthetase. N-acetylglutamate synthase. N-acetylglutamate synthetase. Ornithine acetyltransferase. Ornithine transacetylase. N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L- glutamate. -!- Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity. P74241 P74241 2.7.7.4 Sulfate adenylyltransferase. ATP-sulfurylase. Sulfate adenylate transferase. Sulfurylase. ATP + sulfate = diphosphate + adenylyl sulfate. -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. P74296 P74296 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). P74297 P74297 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P74299 P74299 4.1.1.31 Phosphoenolpyruvate carboxylase. PEP carboxylase. PEPCase. Phosphoenolpyruvic carboxylase. Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-). -!- This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. -!- The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate. P74308 P74308 1.1.1.184 Carbonyl reductase (NADPH). Aldehyde reductase I. NADPH-dependent carbonyl reductase. Prostaglandin 9-ketoreductase. Xenobiotic ketone reductase. R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. -!- Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin, and prostaglandins E and F, reducing them to the corresponding alcohol. -!- Si-specific with respect to NADPH (cf. EC 1.1.1.2). P74309 P74309 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P74334 P74334 1.13.11.75 All-trans-8'-apo-beta-carotenal 15,15'-oxygenase. 8'-apo-beta-carotenal 15,15'-oxygenase. All-trans-8'-apo-beta-carotenal + O(2) = all-trans-retinal + (2E,4E,6E)- 2,6-dimethylocta-2,4,6-trienedial. Fe(2+). -!- The enzyme is involved in retinal biosynthesis in bacteria. -!- Formerly EC 1.14.99.41 and EC 1.14.99.n1. P74352 P74352 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P74421 P74421 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. P74457 P74457 2.7.4.22 UMP kinase. UMP-kinase. UMPK. Uridine monophosphate kinase. Uridylate kinase. ATP + UMP = ADP + UDP. -!- Strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme EC 2.7.4.14 for the same purpose. -!- Subject of feedback regulation, being inhibited by UTP and activated by GTP. P74494 P74494 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. P74507 P74507 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. P74572 P74572 1.5.1.2 Pyrroline-5-carboxylate reductase. P5CR. L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H. -!- Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline. P74582 P74582 4.2.1.3 Aconitate hydratase. Aconitase. Cis-aconitase. Citrate hydro-lyase. Citrate(isocitrate) hydro-lyase. Citrate = isocitrate. Iron-sulfur. -!- Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. -!- The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. -!- Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3- tricarboxylate. -!- Formerly EC 4.2.1.4. P74582 P74582 4.2.1.99 2-methylisocitrate dehydratase. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3- tricarboxylate + H(2)O. -!- The enzyme from the fungus Yarrowia lipolytica does not act on isocitrate. P74618 P74618 3.1.1.31 6-phosphogluconolactonase. 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-phospho-D-gluconate. P74667 P74667 5.1.1.7 Diaminopimelate epimerase. LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. P74689 P74689 4.2.1.9 Dihydroxy-acid dehydratase. 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H(2)O. P74745 P74745 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P75039 P75039 2.7.1.202 Protein-N(pi)-phosphohistidine--D-fructose phosphotransferase. Fructose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-fructose(Side 1) = [protein]-L- histidine + D-fructose 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P75050 P75050 5.4.2.8 Phosphomannomutase. Phosphomannose mutase. Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. -!- Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.7. P75080 P75080 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P75089 P75089 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P75172 P75172 3.6.4.13 RNA helicase. ATP + H(2)O = ADP + phosphate. -!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase). P75206 P75206 3.4.11.1 Leucyl aminopeptidase. Cytosol aminopeptidase. Leucine aminopeptidase. Peptidase S. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Zn(2+). -!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC 3.4.1.1. P75206 P75206 3.4.11.10 Bacterial leucyl aminopeptidase. Aeromonas proteolytica aminopeptidase. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Zn(2+). -!- Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus. -!- Belongs to peptidase families M17 and M28. P75245 P75245 2.7.2.1 Acetate kinase. Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK. ATP + acetate = ADP + acetyl phosphate. Mg(2+). -!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. P75250 P75250 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P75258 P75258 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). P75271 P75271 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P75293 P75293 4.1.1.85 3-dehydro-L-gulonate-6-phosphate decarboxylase. 3-dehydro-L-gulonate-6-phosphate carboxy-lyase. 3-keto-L-gulonate 6-phosphate decarboxylase. KGPDC. 3-dehydro-L-gulonate 6-phosphate = L-xylulose 5-phosphate + CO(2). Mg(2+). -!- Along with EC 5.1.3.22, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli. P75313 P75313 3.4.11.9 Xaa-Pro aminopeptidase. Aminoacylproline aminopeptidase. Aminopeptidase P. Proline aminopeptidase. X-Pro aminopeptidase. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Cobalt cation or Mn(2+). -!- Generally membrane bound enzyme present in both mammalian and bacterial cells. -!- Belongs to peptidase family M24B. P75358 P75358 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. P75359 P75359 2.3.1.8 Phosphate acetyltransferase. Phosphoacylase. Phosphotransacetylase. Acetyl-CoA + phosphate = CoA + acetyl phosphate. -!- Also acts with other short-chain acyl-CoAs. P75386 P75386 3.1.7.2 Guanosine-3',5'-bis(diphosphate) 3'-diphosphatase. (ppGpp)ase. Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase. Penta-phosphate guanosine-3'-diphosphohydrolase. Penta-phosphate guanosine-3'-pyrophosphohydrolase. Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate. P75390 P75390 1.2.4.1 Pyruvate dehydrogenase (acetyl-transferring). MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase. Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. P75393 P75393 1.8.1.4 Dihydrolipoyl dehydrogenase. Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. FAD. -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3. P75394 P75394 6.3.1.20 Lipoate--protein ligase. Lipoate protein ligase. Lipoate-protein ligase A. LPL. ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine = a [lipoyl- carrier protein]-N(6)-(lipoyl)lysine + AMP + diphosphate. Mg(2+). -!- This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid. -!- The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). -!- Lipoylation is essential for the function of these enzymes. -!- The enzyme can also use octanoate instead of lipoate. -!- Formerly EC 2.7.7.63. P75525 P75525 3.1.3.16 Protein-serine/threonine phosphatase. Protein phosphatase-1. Protein phosphatase-2A. Protein phosphatase-2B. Protein phosphatase-2C. Serine/threonine specific protein phosphatase. [a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate. -!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1). P75526 P75526 2.7.4.8 Guanylate kinase. Deoxyguanylate kinase. GMP kinase. Guanosine monophosphate kinase. ATP + GMP = ADP + GDP. -!- dGMP can also act as acceptor. -!- dATP can act as donor. P75569 P75569 2.7.1.199 Protein-N(pi)-phosphohistidine--D-glucose phosphotransferase. D-glucose PTS permease. [Protein]-N(pi)-phospho-L-histidine + D-glucose(Side 1) = [protein]-L- histidine + D-glucose 6-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. P75691 P75691 1.1.1.2 Alcohol dehydrogenase (NADP(+)). Aldehyde reductase (NADPH). An alcohol + NADP(+) = an aldehyde + NADPH. Zn(2+). -!- Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. -!- May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55. -!- Re-specific with respect to NADPH. P75809 P75809 3.1.3.104 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase. 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase. 5-amino-6-(5-phospho-D-ribitylamino)uracil + H(2)O = 5-amino-6- (D-ribitylamino)uracil + phosphate. Mg(2+). -!- The enzyme, which is found in plants and bacteria, is part of a pathway for riboflavin biosynthesis. -!- Most forms of the enzyme has a broad substrate specificity. P75949 P75949 3.2.1.52 Beta-N-acetylhexosaminidase. Beta-hexosaminidase. Hexosaminidase. N-acetyl-beta-glucosaminidase. Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. -!- Acts on N-acetylglucosides and N-acetylgalactosides. -!- Formerly EC 3.2.1.29 and EC 3.2.1.30. P76014 P76014 2.7.1.121 Phosphoenolpyruvate--glycerone phosphotransferase. Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate. P76015 P76015 2.7.1.121 Phosphoenolpyruvate--glycerone phosphotransferase. Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate. P76143 P76143 2.3.1.245 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase. Glycerone phosphate + acetyl-CoA = 3-hydroxy-5-phosphonooxypentane-2,4- dione + coenzyme A. -!- The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2. P76558 P76558 1.1.1.40 Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+)). Malic enzyme. NADP-malic enzyme. Pyruvic-malic carboxylase. (1) (S)-malate + NADP(+) = pyruvate + CO(2) + NADPH. (2) Oxaloacetate = pyruvate + CO(2). -!- The enzyme catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate, cf. EC 1.1.1.38 and EC 1.1.1.39. P77172 P77172 3.1.4.52 Cyclic-guanylate-specific phosphodiesterase. C-di-GMP-specific phosphodiesterase. PDEA1. Phosphodiesterase A1. Cyclic di-3',5'-guanylate + H(2)O = 5'-phosphoguanylyl(3'->5')guanosine. Heme; Mg(2+); Mn(2+). -!- Inhibited by Ca(2+) and Zn(2+). -!- Linearizes cyclic di-3',5'-guanylate, the product of EC 2.7.7.65 and an allosteric activator of EC 2.4.1.12 rendering it inactive. -!- It is the balance between these two enzymes that determines the cellular level of cyclic di-3',5'-guanylate. P77510 P77510 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P77625 P77625 3.1.3.22 Mannitol-1-phosphatase. D-mannitol 1-phosphate + H(2)O = D-mannitol + phosphate. P77625 P77625 3.1.3.23 Sugar-phosphatase. Sugar phosphate + H(2)O = sugar + phosphate. -!- Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate. P77625 P77625 3.1.3.50 Sorbitol-6-phosphatase. Sorbitol 6-phosphate + H(2)O = sorbitol + phosphate. -!- Acts, very slowly, on hexose 6-phosphates. P77650 P77650 1.18.1.3 Ferredoxin--NAD(+) reductase. Reduced ferredoxin + NAD(+) = oxidized ferredoxin + NADH. FAD. -!- The reaction is written for a [2Fe-2S] ferredoxin, which is characteristic of some mono- and dioxygenase systems. -!- some anaerobic bacteria have a 2[4Fe-4S] ferredoxin, which transfers two electrons. P77674 P77674 1.2.1.19 Aminobutyraldehyde dehydrogenase. 1-pyrroline dehydrogenase. 4-aminobutanal dehydrogenase. ABALDH. Gamma-guanidinobutyraldehyde dehydrogenase. 4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH. -!- The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates. -!- The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54). -!- As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. -!- Formerly EC 1.5.1.35. P77756 P77756 6.3.4.20 7-cyano-7-deazaguanine synthase. 7-cyano-7-carbaguanine synthase. PreQ0 synthase. 7-carboxy-7-carbaguanine + NH(3) + ATP = 7-cyano-7-carbaguanine + ADP + phosphate + H(2)O. -!- The reaction is part of the biosynthesis pathway of queuosine. P77961 P77961 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. P77962 P77962 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. P77965 P77965 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P77968 P77968 1.15.1.1 Superoxide dismutase. 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Fe cation or Mn(2+) or (Zn(2+) and Cu cation). P77972 P77972 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. P77973 P77973 6.3.4.5 Argininosuccinate synthase. Arginine succinate synthetase. Argininosuccinate synthetase. Citrulline--aspartate ligase. ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate. P78010 P78010 5.3.1.1 Triose-phosphate isomerase. Phosphotriose isomerase. Triose phosphoisomerase. Triosephosphate isomerase. Triosephosphate mutase. D-glyceraldehyde 3-phosphate = glycerone phosphate. P78018 P78018 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. P78027 P78027 1.17.4.1 Ribonucleoside-diphosphate reductase. Ribonucleotide reductase. 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Fe(3+) or adenosylcob(III)alamin or Mn(2+). -!- This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. -!- There are three types of this enzyme differing in their cofactors. -!- Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. -!- In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6 and EC 1.17.4.2. P78028 P78028 1.5.1.3 Dihydrofolate reductase. Tetrahydrofolate dehydrogenase. 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. -!- The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate. -!- Formerly EC 1.5.1.4. P78032 P78032 5.6.2.2 DNA topoisomerase. DNA topoisomerase I. Nicking-closing enzyme. Omega-protein. Relaxing enzyme. Swivelase. Type I DNA topoisomerase. Untwisting enzyme. ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. -!- These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.6.2.3. -!- Formerly EC 5.99.1.2. P78285 P78285 3.2.1.17 Lysozyme. Muramidase. Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl- D-glucosamine residues in chitodextrins. -!- Cf. EC 3.2.1.14. P80046 P80046 1.1.1.42 Isocitrate dehydrogenase (NADP(+)). Dual-cofactor-specific isocitrate dehydrogenase. IDH. IDP. Isocitrate (NADP) dehydrogenase. Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Isocitrate dehydrogenase (NADP). Isocitrate dehydrogenase (NADP-dependent). NADP isocitric dehydrogenase. NADP(+)-ICDH. NADP(+)-IDH. NADP(+)-linked isocitrate dehydrogenase. NADP-dependent isocitrate dehydrogenase. NADP-dependent isocitric dehydrogenase. NADP-linked isocitrate dehydrogenase. NADP-specific isocitrate dehydrogenase. Oxalosuccinate decarboxylase. Oxalsuccinic decarboxylase. Triphosphopyridine nucleotide-linked isocitrate dehydrogenase- oxalosuccinate carboxylase. Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Mn(2+) or Mg(2+). -!- Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate. -!- In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. -!- The enzyme from some species can also use NAD(+) but much more slowly. P80239 P80239 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P80244 P80244 3.4.21.92 Endopeptidase Clp. Caseinolytic protease. Endopeptidase Ti. Protease Ti. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). -!- Belongs to peptidase family S14. P80505 P80505 1.2.1.59 Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating). NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase (NAD(P)(+)). Triosephosphate dehydrogenase (NAD(P)). D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D- glyceroyl phosphate + NAD(P)H. -!- NAD(+) and NADP(+) can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 and EC 1.2.1.13, which are NAD(+)- and NADP(+)- dependent, respectively. P80507 P80507 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P80698 P80698 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. P80858 P80858 4.2.1.33 3-isopropylmalate dehydratase. (2R,3S)-3-isopropylmalate hydro-lyase. 3-isopropylmalate hydro-lyase. Alpha-IPM isomerase. Isopropylmalate isomerase. (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. Iron-sulfur. -!- Forms part of the leucine-biosynthesis pathway. -!- Brings about the interconversion of the two isomers of isopropylmalate. P80859 P80859 1.1.1.44 Phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating). 6-phosphogluconic carboxylase. 6-phosphogluconic dehydrogenase. 6PGD. Phosphogluconic acid dehydrogenase. 6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH. -!- The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. -!- Highly specific for NADP(+). -!- Cf. EC 1.1.1.343. P80860 P80860 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. P80865 P80865 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P80877 P80877 2.1.1.14 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. Cobalamin-independent methionine synthase. Homocysteine methylase. Methionine synthase (cobalamin-independent). Methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase. Tetrahydropteroylglutamate-homocysteine transmethylase. 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. Zn(2+). -!- Requires phosphate. -!- The enzyme from Escherichia coli also requires a reducing system. -!- Unlike EC 2.1.1.13 this enzyme does not contain cobalamin. P80885 P80885 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). P80886 P80886 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P81181 P81181 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. P94335 P94335 6.3.2.8 UDP-N-acetylmuramate--L-alanine ligase. Alanine-adding enzyme. L-Ala ligase. L-alanine-adding enzyme. MurC synthetase. UDP-acetylmuramyl-L-alanine synthetase. UDP-MurNAc:L-alanine ligase. UDP-N-acetylmuramoyl-L-alanine synthetase. UDP-N-acetylmuramoylalanine synthetase. UDP-N-acetylmuramyl:L-alanine ligase. UDPMurNAc-L-alanine synthetase. Uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase. Uridine diphosphate N-acetylmuramate:L-alanine ligase. Uridine diphospho-N-acetylmuramoylalanine synthetase. Uridine-diphosphate-N-acetylmuramate:L-alanine ligase. ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP- N-acetyl-alpha-D-muramoyl-L-alanine. -!- Involved in the synthesis of a cell-wall peptide. P94417 P94417 2.7.2.4 Aspartate kinase. Aspartokinase. ATP + L-aspartate = ADP + 4-phospho-L-aspartate. -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3. -!- This is also the case for two of the four isoenzymes in Arabidopsis thaliana. -!- The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction. P94547 P94547 6.2.1.3 Long-chain-fatty-acid--CoA ligase. Acyl-activating enzyme. Acyl-CoA synthetase. Fatty acid thiokinase (long chain). Lignoceroyl-CoA synthase. ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. -!- Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. -!- The liver enzyme acts on acids from C(6) to C(20); that from brain shows high activity up to C(24). P94549 P94549 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). P94565 P94565 2.3.3.13 2-isopropylmalate synthase. 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating). Alpha-IPM synthetase. Alpha-isopropylmalate synthase. Alpha-isopropylmalate synthetase. Alpha-isopropylmalic synthetase. Isopropylmalate synthase. Isopropylmalate synthetase. Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA. K(+). -!- Formerly EC 4.1.3.12. P95189 P95189 3.1.3.15 Histidinol-phosphatase. L-histidinol phosphate + H(2)O = L-histidinol + phosphate. P95690 P95690 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P95867 P95867 3.2.1.141 4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase. Malto-oligosyltrehalose trehalohydrolase. Maltooligosyl trehalose trehalohydrolase. Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)- alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D- glucan. P95907 P95907 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. P95931 P95931 3.1.3.18 Phosphoglycolate phosphatase. 2-phosphoglycolate + H(2)O = glycolate + phosphate. P95968 P95968 6.1.1.17 Glutamate--tRNA ligase. Glutamic acid translase. Glutamyl-tRNA synthetase. ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). P95970 P95970 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). P95979 P95979 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. P96041 P96041 6.1.1.7 Alanine--tRNA ligase. Alanine translase. Alanyl-tRNA synthetase. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). P96076 P96076 4.1.1.23 Orotidine-5'-phosphate decarboxylase. OMP decarboxylase. OMPdcase. Orotidine-5'-phosphate carboxy-lyase. Orotidylic decarboxylase. UMP synthase. Uridine 5'-monophosphate synthase. Orotidine 5'-phosphate = UMP + CO(2). -!- The enzyme from higher eukaryotes is identical with EC 2.4.2.10. P96218 P96218 1.4.1.13 Glutamate synthase (NADPH). Glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase. Glutamate synthetase (NADP). Glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP). Glutamine-ketoglutaric aminotransferase. GOGAT. L-glutamate synthase. L-glutamate synthetase. NADPH-dependent glutamate synthase. NADPH-glutamate synthase. 2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH. FAD; FMN; Iron-sulfur. -!- The reaction takes place in the opposite direction. -!- The protein is composed of two subunits, alpha and beta. -!- The alpha subunit is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4). -!- The beta subunit transfers electrons to the cosubstrate. -!- The NH(3) is channeled through a 31 A channel in the active protein. -!- In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can be produced. -!- In the intact alpha-beta complex, ammonia production only takes place as part of the overall reaction. -!- Formerly EC 2.6.1.53. P96374 P96374 3.6.1.11 Exopolyphosphatase. Exopolypase. Metaphosphatase. (Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate. P96613 P96613 6.3.2.10 UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase. MurF synthetase. UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase. UDP-MurNAc-pentapeptide synthetase. UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine synthetase. UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D- alanyl-D-alanine synthetase. UDP-N-acetylmuramoylalanine-D-glutamyl-lysine--D-alanyl-D-alanine ligase. UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D- alanine ligase. UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine ligase. UDPacetylmuramoylpentapeptide synthetase. Uridine diphosphoacetylmuramoylpentapeptide synthetase. ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl- D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D- glutamyl-L-lysyl-D-alanyl-D-alanine. -!- Involved with EC 6.3.2.4, EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8 and EC 6.3.2.9 in the synthesis of a cell-wall peptide. -!- Also catalyzes the reaction when the C-terminal residue of the tripeptide is meso-2,4-diaminoheptanedioate (acylated at its L-center), linking the D-Ala--D-Ala to the carboxy group of the L-center. -!- Formerly EC 6.3.2.15. P96716 P96716 2.7.10.2 Non-specific protein-tyrosine kinase. Cytoplasmic protein tyrosine kinase. ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. -!- Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain. -!- In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families. -!- Formerly EC 2.7.1.112. P96718 P96718 1.1.1.22 UDP-glucose 6-dehydrogenase. UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH. -!- Also acts on UDP-2-deoxyglucose. P9WF29 P9WF29 3.1.11.6 Exodeoxyribonuclease VII. E.coli exonuclease VII. Exonuclease VII. Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates. -!- Preference for single-stranded DNA. -!- Similar enzyme: Micrococcus luteus exonuclease. P9WFW9 P9WFW9 5.4.4.2 Isochorismate synthase. Isochorismate mutase. Isochorismate synthetase. Chorismate = isochorismate. Mg(2+). -!- The reaction is reversible. -!- Formerly EC 5.4.99.6. P9WFX5 P9WFX5 2.4.2.18 Anthranilate phosphoribosyltransferase. Phosphoribosyl-anthranilate diphosphorylase. Phosphoribosyl-anthranilate pyrophosphorylase. N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate. -!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20 and EC 5.3.1.24). P9WFX7 P9WFX7 4.1.1.48 Indole-3-glycerol-phosphate synthase. Indoleglycerol phosphate synthetase. 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C- (3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. -!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.3.27, EC 4.2.1.20 and EC 5.3.1.24). P9WFZ1 P9WFZ1 2.1.1.220 tRNA (adenine(58)-N(1))-methyltransferase. tRNA (m(1)A(58)) methyltransferase. tRNA m(1)A(58) methyltransferase. S-adenosyl-L-methionine + adenine(58) in tRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(58) in tRNA. -!- The enzyme specifically methylates adenine(58) in tRNA. -!- The methylation of A(58) is critical for maintaining the stability of initiator tRNA(Met) in yeast. -!- Formerly EC 2.1.1.36. P9WG33 P9WG33 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. P9WG38 P9WG38 2.2.1.6 Acetolactate synthase. Acetohydroxy acid synthetase. Acetohydroxyacid synthase. Acetolactate pyruvate-lyase (carboxylating). Acetolactic synthetase. Alpha-acetohydroxy acid synthetase. Alpha-acetohydroxyacid synthase. Alpha-acetolactate synthase. Alpha-acetolactate synthetase. 2 pyruvate = 2-acetolactate + CO(2). Thiamine diphosphate. -!- The reaction shown is in the pathway of biosynthesis of valine. -!- The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine. -!- Formerly EC 4.1.3.18. P9WG39 P9WG39 2.2.1.6 Acetolactate synthase. Acetohydroxy acid synthetase. Acetohydroxyacid synthase. Acetolactate pyruvate-lyase (carboxylating). Acetolactic synthetase. Alpha-acetohydroxy acid synthetase. Alpha-acetohydroxyacid synthase. Alpha-acetolactate synthase. Alpha-acetolactate synthetase. 2 pyruvate = 2-acetolactate + CO(2). Thiamine diphosphate. -!- The reaction shown is in the pathway of biosynthesis of valine. -!- The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine. -!- Formerly EC 4.1.3.18. P9WG45 P9WG45 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P9WG47 P9WG47 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. P9WG48 P9WG48 5.6.2.2 DNA topoisomerase. DNA topoisomerase I. Nicking-closing enzyme. Omega-protein. Relaxing enzyme. Swivelase. Type I DNA topoisomerase. Untwisting enzyme. ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. -!- These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.6.2.3. -!- Formerly EC 5.99.1.2. P9WG49 P9WG49 5.6.2.2 DNA topoisomerase. DNA topoisomerase I. Nicking-closing enzyme. Omega-protein. Relaxing enzyme. Swivelase. Type I DNA topoisomerase. Untwisting enzyme. ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. -!- These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.6.2.3. -!- Formerly EC 5.99.1.2. P9WG74 P9WG74 2.5.1.3 Thiamine phosphate synthase. Thiamine-phosphate diphosphorylase. Thiamine-phosphate pyrophosphorylase. Thiamine-phosphate synthase. TMP diphosphorylase. TMP pyrophosphorylase. (1) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy- 4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (2) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4- methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (3) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5- (2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. -!- The enzyme catalyzes the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. -!- The enzyme is thought to accept the product of EC 2.8.1.10 as its substrate. -!- However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, EC 5.3.99.10 converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. -!- In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products. -!- In yeast this activity is found in a bifunctional enzyme and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme. P9WG75 P9WG75 2.5.1.3 Thiamine phosphate synthase. Thiamine-phosphate diphosphorylase. Thiamine-phosphate pyrophosphorylase. Thiamine-phosphate synthase. TMP diphosphorylase. TMP pyrophosphorylase. (1) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy- 4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (2) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4- methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (3) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5- (2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. -!- The enzyme catalyzes the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. -!- The enzyme is thought to accept the product of EC 2.8.1.10 as its substrate. -!- However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, EC 5.3.99.10 converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. -!- In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products. -!- In yeast this activity is found in a bifunctional enzyme and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme. P9WGC7 P9WGC7 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. P9WGE7 P9WGE7 1.15.1.1 Superoxide dismutase. 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Fe cation or Mn(2+) or (Zn(2+) and Cu cation). P9WGJ3 P9WGJ3 3.1.3.3 Phosphoserine phosphatase. O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate. P9WGK1 P9WGK1 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGK3 P9WGK3 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGK4 P9WGK4 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGK5 P9WGK5 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGK8 P9WGK8 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGK9 P9WGK9 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGL3 P9WGL3 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGL5 P9WGL5 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. P9WGR0 P9WGR0 1.3.1.9 Enoyl-[acyl-carrier-protein] reductase (NADH). Enoyl-ACP reductase. NADH-enoyl acyl carrier protein reductase. NADH-specific enoyl-ACP reductase. An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH. -!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons. P9WGR1 P9WGR1 1.3.1.9 Enoyl-[acyl-carrier-protein] reductase (NADH). Enoyl-ACP reductase. NADH-enoyl acyl carrier protein reductase. NADH-specific enoyl-ACP reductase. An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH. -!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons. P9WGT2 P9WGT2 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH. -!- Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates. P9WGT3 P9WGT3 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH. -!- Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates. P9WGV2 P9WGV2 3.3.1.1 Adenosylhomocysteinase. Adenosylhomocysteine hydrolase. AdoHcyase. S-adenosylhomocysteinase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine synthase. SAHase. S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine. NAD(+). -!- The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4. P9WGV3 P9WGV3 3.3.1.1 Adenosylhomocysteinase. Adenosylhomocysteine hydrolase. AdoHcyase. S-adenosylhomocysteinase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine synthase. SAHase. S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine. NAD(+). -!- The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4. P9WGY8 P9WGY8 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P9WGY9 P9WGY9 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P9WGZ1 P9WGZ1 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. P9WH05 P9WH05 3.6.4.13 RNA helicase. ATP + H(2)O = ADP + phosphate. -!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase). P9WH07 P9WH07 2.1.1.182 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase. 4 S-adenosyl-L-methionine + adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(1518)/N(6)- dimethyladenine(1519) in 16S rRNA. -!- KsgA introduces the most highly conserved ribosomal RNA modification, the dimethylation of adenine(1518) and adenine(1519) in 16S rRNA. -!- Strains lacking the methylase are resistant to kasugamycin. -!- Formerly EC 2.1.1.48. P9WHG9 P9WHG9 2.7.6.5 GTP diphosphokinase. GTP pyrophosphokinase. Guanosine 3',5'-polyphosphate synthase. ppGpp synthetase I. Stringent factor. ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. -!- GDP can also act as acceptor. P9WHG9 P9WHG9 3.1.7.2 Guanosine-3',5'-bis(diphosphate) 3'-diphosphatase. (ppGpp)ase. Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase. Penta-phosphate guanosine-3'-diphosphohydrolase. Penta-phosphate guanosine-3'-pyrophosphohydrolase. Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate. P9WHK5 P9WHK5 2.7.4.22 UMP kinase. UMP-kinase. UMPK. Uridine monophosphate kinase. Uridylate kinase. ATP + UMP = ADP + UDP. -!- Strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme EC 2.7.4.14 for the same purpose. -!- Subject of feedback regulation, being inhibited by UTP and activated by GTP. P9WHK7 P9WHK7 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. P9WHM1 P9WHM1 5.4.99.18 5-(carboxyamino)imidazole ribonucleotide mutase. N(5)-CAIR mutase. N(5)-carboxyaminoimidazole ribonucleotide mutase. 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate. -!- In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates. -!- In the absence of EC 6.3.2.6, the reaction is reversible. -!- The substrate is readily converted into 5-amino-1-(5-phospho-D- ribosyl)imidazole by non-enzymic decarboxylation. P9WHS1 P9WHS1 3.13.1.6 [CysO sulfur-carrier protein]-S-L-cysteine hydrolase. [CysO]-cysteine peptidase. Metallocarboxypeptidase Mec. [CysO sulfur-carrier protein]-Gly-NH-CH(2)-C(O)-S-L-cysteine + H(2)O = [CysO sulfur-carrier protein]-Gly-NH-CH(2)-COOH + L-cysteine. Zn(2+). -!- The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in an L-cysteine biosynthesis pathway. -!- It acts on the product of EC 2.5.1.113. P9WHT2 P9WHT2 3.4.11.1 Leucyl aminopeptidase. Cytosol aminopeptidase. Leucine aminopeptidase. Peptidase S. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Zn(2+). -!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC 3.4.1.1. P9WHT2 P9WHT2 3.4.11.10 Bacterial leucyl aminopeptidase. Aeromonas proteolytica aminopeptidase. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Zn(2+). -!- Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus. -!- Belongs to peptidase families M17 and M28. P9WHT3 P9WHT3 3.4.11.1 Leucyl aminopeptidase. Cytosol aminopeptidase. Leucine aminopeptidase. Peptidase S. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Zn(2+). -!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC 3.4.1.1. P9WHT3 P9WHT3 3.4.11.10 Bacterial leucyl aminopeptidase. Aeromonas proteolytica aminopeptidase. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Zn(2+). -!- Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus. -!- Belongs to peptidase families M17 and M28. P9WHU1 P9WHU1 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. P9WHU7 P9WHU7 1.5.1.2 Pyrroline-5-carboxylate reductase. P5CR. L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H. -!- Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline. P9WHV0 P9WHV0 1.2.1.41 Glutamate-5-semialdehyde dehydrogenase. Beta-glutamylphosphate reductase. Gamma-glutamylphosphate reductase. Glutamyl-gamma-semialdehyde dehydrogenase. L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH. P9WHV1 P9WHV1 1.2.1.41 Glutamate-5-semialdehyde dehydrogenase. Beta-glutamylphosphate reductase. Gamma-glutamylphosphate reductase. Glutamyl-gamma-semialdehyde dehydrogenase. L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH. P9WHV7 P9WHV7 2.7.1.23 NAD(+) kinase. DPN kinase. ATP + NAD(+) = ADP + NADP(+). P9WHW3 P9WHW3 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. P9WHW5 P9WHW5 3.1.3.16 Protein-serine/threonine phosphatase. Protein phosphatase-1. Protein phosphatase-2A. Protein phosphatase-2B. Protein phosphatase-2C. Serine/threonine specific protein phosphatase. [a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate. -!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1). P9WI55 P9WI55 3.6.1.1 Inorganic diphosphatase. Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase. Diphosphate + H(2)O = 2 phosphate. -!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. -!- Cf. EC 7.1.3.1. P9WI62 P9WI62 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI63 P9WI63 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI64 P9WI64 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI65 P9WI65 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI66 P9WI66 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI67 P9WI67 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI69 P9WI69 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI70 P9WI70 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI71 P9WI71 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI72 P9WI72 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI73 P9WI73 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI74 P9WI74 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI75 P9WI75 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI76 P9WI76 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI77 P9WI77 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI78 P9WI78 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI79 P9WI79 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI80 P9WI80 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI81 P9WI81 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI82 P9WI82 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WI83 P9WI83 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. P9WIA1 P9WIA1 3.1.3.48 Protein-tyrosine-phosphatase. Phosphotyrosine phosphatase. PTPase. Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. -!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2. P9WIC5 P9WIC5 4.1.3.40 Chorismate lyase. CL. CPL. Chorismate = 4-hydroxybenzoate + pyruvate. -!- Catalyzes the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria. -!- The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine. P9WIC7 P9WIC7 3.1.3.70 Mannosyl-3-phosphoglycerate phosphatase. 2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H(2)O = 2-O-(alpha-D- mannosyl)-D-glycerate + phosphate. Mg(2+). -!- The enzyme from Pyrococcus horikoshii is specific for alpha-D- mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate. P9WIC7 P9WIC7 3.1.3.85 Glucosyl-3-phosphoglycerate phosphatase. 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H(2)O = 2-O-(alpha- D-glucopyranosyl)-D-glycerate + phosphate. -!- The enzyme is involved in biosynthesis of 2-O-(alpha-D- glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 catalyzes the conversion of GDP-glucose and 3-phospho-D- glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. -!- In vivo the enzyme catalyzes the dephosphorylation of 2-O-(alpha-D- mannopyranosyl)-3-phospho-D-glycerate with lower efficiency. -!- Divalent metal ions (Mg(2+), Mn(2+) or Co(2+)) stimulate activity. P9WID5 P9WID5 2.7.1.20 Adenosine kinase. ATP + adenosine = ADP + AMP. -!- 2-aminoadenosine can also act as acceptor. P9WIE3 P9WIE3 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. P9WIE5 P9WIE5 1.11.1.21 Catalase peroxidase. (1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O. -!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. P9WIH2 P9WIH2 4.1.1.32 Phosphoenolpyruvate carboxykinase (GTP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2). -!- ITP can act as phosphate donor. P9WIH3 P9WIH3 4.1.1.32 Phosphoenolpyruvate carboxykinase (GTP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2). -!- ITP can act as phosphate donor. P9WII8 P9WII8 4.3.3.6 Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing). D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate. -!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants. P9WII9 P9WII9 4.3.3.6 Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing). D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate. -!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants. P9WIN1 P9WIN1 2.7.1.2 Glucokinase. Glucose kinase. ATP + D-glucose = ADP + D-glucose 6-phosphate. -!- A group of enzymes found in invertebrates and microorganisms highly specific for glucose. P9WIN1 P9WIN1 2.7.1.63 Polyphosphate--glucose phosphotransferase. Polyphosphate glucokinase. (Phosphate)(n) + D-glucose = (phosphate)(n-1) + D-glucose 6-phosphate. -!- Requires a neutral salt, e.g. KCl, for maximum activity. -!- Also acts on glucosamine. P9WIP3 P9WIP3 2.5.1.74 1,4-dihydroxy-2-naphthoate polyprenyltransferase. An all-trans-polyprenyl diphosphate + 1,4-dihydroxy-2-naphthoate = a demethylmenaquinol + diphosphate + CO(2). -!- This enzyme catalyzes a step in the synthesis of menaquinone, in which the prenyl chain synthesized by polyprenyl diphosphate synthase is transferred to 1,4-dihydroxy-2-naphthoate (DHNA). -!- The bacterial enzyme is an inner membrane protein, with the C-terminus located in the periplasm. -!- It is highly specific for DHNA but not for a specific length of the prenyl chain. P9WIS5 P9WIS5 1.2.4.2 Oxoglutarate dehydrogenase (succinyl-transferring). 2-ketoglutarate dehydrogenase. 2-oxoglutarate dehydrogenase. 2-oxoglutarate: lipoate oxidoreductase. 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- succinylating). AKGDH. Alpha-ketoglutarate dehydrogenase. Alpha-ketoglutaric acid dehydrogenase. Alpha-ketoglutaric dehydrogenase. Alpha-oxoglutarate dehydrogenase. Ketoglutaric dehydrogenase. OGDC. Oxoglutarate decarboxylase. Oxoglutarate dehydrogenase. Oxoglutarate dehydrogenase (lipoamide). 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61. P9WIS5 P9WIS5 2.2.1.5 2-hydroxy-3-oxoadipate synthase. 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating). 2-hydroxy-3-oxoadipate synthetase. Alpha-ketoglutaric-glyoxylic carboligase. Oxoglutarate: glyoxylate carboligase. 2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2). Thiamine diphosphate. -!- The product decarboxylates to 5-hydroxy-4-oxopentanoate. -!- The enzyme can decarboxylate 2-oxoglutarate. -!- Acetaldehyde can replace glyoxylate. -!- Formerly EC 4.1.3.15. P9WIS5 P9WIS5 2.3.1.61 Dihydrolipoyllysine-residue succinyltransferase. Dihydrolipoamide S-succinyltransferase. Dihydrolipoamide succinyltransferase. Dihydrolipoic transsuccinylase. Dihydrolipolyl transsuccinylase. Dihydrolipoyl transsuccinylase. Lipoate succinyltransferase. Lipoic transsuccinylase. Lipoyl transsuccinylase. Succinyl-CoA:dihydrolipoamide S-succinyltransferase. Succinyl-CoA:dihydrolipoate S-succinyltransferase. Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine. -!- A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A. P9WIS5 P9WIS5 4.1.1.71 2-oxoglutarate decarboxylase. 2-oxoglutarate carboxy-lyase. Alpha-ketoglutarate decarboxylase. 2-oxoglutarate = succinate semialdehyde + CO(2). Thiamine diphosphate. -!- Highly specific. P9WJH6 P9WJH6 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. P9WJH7 P9WJH7 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. P9WJL7 P9WJL7 6.3.2.8 UDP-N-acetylmuramate--L-alanine ligase. Alanine-adding enzyme. L-Ala ligase. L-alanine-adding enzyme. MurC synthetase. UDP-acetylmuramyl-L-alanine synthetase. UDP-MurNAc:L-alanine ligase. UDP-N-acetylmuramoyl-L-alanine synthetase. UDP-N-acetylmuramoylalanine synthetase. UDP-N-acetylmuramyl:L-alanine ligase. UDPMurNAc-L-alanine synthetase. Uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase. Uridine diphosphate N-acetylmuramate:L-alanine ligase. Uridine diphospho-N-acetylmuramoylalanine synthetase. Uridine-diphosphate-N-acetylmuramate:L-alanine ligase. ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP- N-acetyl-alpha-D-muramoyl-L-alanine. -!- Involved in the synthesis of a cell-wall peptide. P9WJM3 P9WJM3 3.2.2.9 Adenosylhomocysteine nucleosidase. 5'-methyladenosine nucleosidase. AdoHcy/MTA nucleosidase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine nucleosidase. S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. S-adenosyl-L-homocysteine + H(2)O = S-(5-deoxy-D-ribos-5-yl)-L- homocysteine + adenine. P9WJP1 P9WJP1 2.1.1.199 16S rRNA (cytosine(1402)-N(4))-methyltransferase. S-adenosyl-L-methionine + cytosine(1402) in 16S rRNA = S-adenosyl-L- homocysteine + N(4)-methylcytosine(1402) in 16S rRNA. -!- RsmH catalyzes the N(4)-methylation of cytosine(1402) and RsmI (EC 2.1.1.198) catalyzes the 2'-O-methylation of cytosine(1402) in 16S rRNA. -!- Both methylations are necessary for efficient translation initiation at the UUG and GUG codons. P9WJQ7 P9WJQ7 2.10.1.1 Molybdopterin molybdotransferase. Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP. Zn(2+) or Mg(2+). -!- Catalyzes the insertion of molybdenum into the ene-dithiol group of molybdopterin. -!- In eukaryotes this reaction is catalyzed by the N-terminal domain of a fusion protein whose C-terminal domain catalyzes EC 2.7.7.75. P9WJQ9 P9WJQ9 2.7.7.77 Molybdenum cofactor guanylyltransferase. MoCo guanylyltransferase. GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor. -!- Catalyzes the guanylation of the molybdenum cofactor. -!- This modification occurs only in prokaryotes. P9WJR9 P9WJR9 4.6.1.17 Cyclic pyranopterin monophosphate synthase. (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate. -!- The enzyme catalyzes an early step in the biosynthesis of the molybdenum cofactor (MoCo). -!- Formerly EC 4.1.99.18. P9WJY9 P9WJY9 2.3.1.31 Homoserine O-acetyltransferase. Homoserine O-trans-acetylase. Homoserine transacetylase. Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine. P9WK07 P9WK07 2.1.1.14 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. Cobalamin-independent methionine synthase. Homocysteine methylase. Methionine synthase (cobalamin-independent). Methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase. Tetrahydropteroylglutamate-homocysteine transmethylase. 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. Zn(2+). -!- Requires phosphate. -!- The enzyme from Escherichia coli also requires a reducing system. -!- Unlike EC 2.1.1.13 this enzyme does not contain cobalamin. P9WK13 P9WK13 1.1.1.37 Malate dehydrogenase. Malic dehydrogenase. (S)-malate + NAD(+) = oxaloacetate + NADH. -!- Also oxidizes some other 2-hydroxydicarboxylic acids. P9WK17 P9WK17 2.3.3.9 Malate synthase. Glyoxylate transacetase. Glyoxylate transacetylase. Glyoxylic transacetase. L-malate glyoxylate-lyase (CoA-acetylating). Malate condensing enzyme. Malate synthetase. Malic synthetase. Malic-condensing enzyme. Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA. -!- The enzyme catalyzes the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. -!- Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO(2). -!- Formerly EC 4.1.3.2. P9WK24 P9WK24 1.1.1.38 Malate dehydrogenase (oxaloacetate-decarboxylating). Malic enzyme. NAD-malic enzyme. Pyruvic-malic carboxylase. (1) (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. (2) Oxaloacetate = pyruvate + CO(2). -!- Unlike EC 1.1.1.39, this enzyme can also decarboxylate oxaloacetate, cf. EC 1.1.1.40. P9WK25 P9WK25 1.1.1.38 Malate dehydrogenase (oxaloacetate-decarboxylating). Malic enzyme. NAD-malic enzyme. Pyruvic-malic carboxylase. (1) (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. (2) Oxaloacetate = pyruvate + CO(2). -!- Unlike EC 1.1.1.39, this enzyme can also decarboxylate oxaloacetate, cf. EC 1.1.1.40. P9WK87 P9WK87 3.1.1.1 Carboxylesterase. Ali-esterase. B-esterase. Cocaine esterase. Methylbutyrase. Monobutyrase. Procaine esterase. A carboxylic ester + H(2)O = an alcohol + a carboxylate. -!- Wide specificity; also hydrolyzes vitamin A esters. -!- The enzymes from microsomes also catalyze the reactions of EC 3.1.1.2, EC 3.1.1.5, EC 3.1.1.6, EC 3.1.1.23, EC 3.1.1.28, EC 3.1.2.2, EC 3.5.1.4 and EC 3.5.1.13. -!- Formerly EC 3.1.1.12. P9WK93 P9WK93 2.5.1.145 Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase. L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine = sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L- cysteine. -!- This bacterial enzyme, which is associated with the membrane, catalyzes the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the prospective N-terminal cysteine of a prolipoprotein, the first step in the formation of mature triacylated lipoproteins. P9WK95 P9WK95 4.2.1.33 3-isopropylmalate dehydratase. (2R,3S)-3-isopropylmalate hydro-lyase. 3-isopropylmalate hydro-lyase. Alpha-IPM isomerase. Isopropylmalate isomerase. (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. Iron-sulfur. -!- Forms part of the leucine-biosynthesis pathway. -!- Brings about the interconversion of the two isomers of isopropylmalate. P9WK99 P9WK99 3.4.23.36 Signal peptidase II. Bacterial leader peptidase I. Lipoprotein signal peptidase. Premurein-leader peptidase. Prolipoprotein-signal peptidase. SPase II. Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. -!- Inhibited by pepstatin and the antibiotic globomycin. -!- Belongs to peptidase family A8. -!- Formerly EC 3.4.99.35. P9WKA4 P9WKA4 2.3.1.20 Diacylglycerol O-acyltransferase. Diglyceride acyltransferase. Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. -!- Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. P9WKA5 P9WKA5 2.3.1.20 Diacylglycerol O-acyltransferase. Diglyceride acyltransferase. Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. -!- Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. P9WKD3 P9WKD3 3.5.2.6 Beta-lactamase. Cephalosporinase. Penicillinase. A beta-lactam + H(2)O = a substituted beta-amino acid. Zn(2+). -!- Zinc is only requires in class-B enzymes. -!- A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. -!- Formerly EC 3.5.2.8. P9WKE5 P9WKE5 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). P9WKE8 P9WKE8 2.7.4.8 Guanylate kinase. Deoxyguanylate kinase. GMP kinase. Guanosine monophosphate kinase. ATP + GMP = ADP + GDP. -!- dGMP can also act as acceptor. -!- dATP can act as donor. P9WKE9 P9WKE9 2.7.4.8 Guanylate kinase. Deoxyguanylate kinase. GMP kinase. Guanosine monophosphate kinase. ATP + GMP = ADP + GDP. -!- dGMP can also act as acceptor. -!- dATP can act as donor. P9WKF4 P9WKF4 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. P9WKF5 P9WKF5 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. P9WKG3 P9WKG3 1.17.7.3 (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin). (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase. (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H(2)O + oxidized flavodoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin. -!- Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria. -!- Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1). P9WKH1 P9WKH1 2.5.1.10 (2E,6E)-farnesyl diphosphate synthase. Farnesyl pyrophosphate synthetase. Farnesyl-diphosphate synthase. FPP synthetase. Geranyltranstransferase. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)- farnesyl diphosphate. -!- Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. -!- The enzyme will not accept larger prenyl diphosphates as efficient donors. P9WLH5 P9WLH5 3.1.3.73 Adenosylcobalamin/alpha-ribazole phosphatase. Adenosylcobalamin phosphatase. Alpha-ribazole phosphatase. (1) Adenosylcobalamin 5'-phosphate + H(2)O = coenzyme B12 + phosphate. (2) Alpha-ribazole 5'-phosphate + H(2)O = alpha-ribazole + phosphate. -!- This enzyme catalyzes the last step in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, characterized in Salmonella enterica. -!- It also participates in a salvage pathway that recycles cobinamide into adenosylcobalamin. P9WLH5 P9WLH5 3.1.26.4 Ribonuclease H. Endoribonuclease H. RNase H. Endonucleolytic cleavage to 5'-phosphomonoester. -!- Acts on RNA-DNA hybrids. P9WMB5 P9WMB5 2.3.1.265 Phosphatidylinositol dimannoside acyltransferase. PIM2 acyltransferase. (1) An acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo- inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1- phosphatidyl-1D-myo-inositol. (2) An acyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol. -!- The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs). P9WML8 P9WML8 4.2.1.19 Imidazoleglycerol-phosphate dehydratase. D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2- oxopropyl phosphate + H(2)O. P9WML9 P9WML9 4.2.1.19 Imidazoleglycerol-phosphate dehydratase. D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2- oxopropyl phosphate + H(2)O. P9WMM3 P9WMM3 4.3.2.10 Imidazole glycerol-phosphate synthase. IGP synthase. 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho- beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1- (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1- (imidazol-4-yl)glycerol 3-phosphate + L-glutamate. -!- The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. -!- The enzymes from archaea and bacteria are heterodimeric. -!- A glutaminase component (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. -!- The glutminase subunit is only active within the dimeric complex. -!- In fungi and plants the two subunits are combined into a single polypeptide. P9WMN9 P9WMN9 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. P9WMQ1 P9WMQ1 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P9WMQ6 P9WMQ6 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P9WMQ7 P9WMQ7 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). P9WMW1 P9WMW1 2.4.1.1 Glycogen phosphorylase. Amylophosphorylase. Muscle phosphorylase a and b. Polyphosphorylase. ((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. -!- This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. -!- Some of these enzymes catalyze the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. -!- The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. -!- The description (accepted name) of the enzyme should be modified for each specific instance by substituting 'glycogen' with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc. P9WN21 P9WN21 3.1.3.11 Fructose-bisphosphatase. Fructose 1,6-bisphosphatase. Hexose diphosphatase. D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. -!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. P9WN26 P9WN26 2.7.7.42 [Glutamine synthetase] adenylyltransferase. [Glutamate--ammonia-ligase] adenylyltransferase. Glutamate-ammonia-ligase adenylyltransferase. Glutamine-synthetase adenylyltransferase. ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine. -!- This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89). -!- The two activities are present on separate domains. P9WN26 P9WN26 2.7.7.89 [Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase. [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP. -!- This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42). -!- The two activities are present on separate domains. -!- Formerly EC 3.1.4.15. P9WN27 P9WN27 2.7.7.42 [Glutamine synthetase] adenylyltransferase. [Glutamate--ammonia-ligase] adenylyltransferase. Glutamate-ammonia-ligase adenylyltransferase. Glutamine-synthetase adenylyltransferase. ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine. -!- This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89). -!- The two activities are present on separate domains. P9WN27 P9WN27 2.7.7.89 [Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase. [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP. -!- This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42). -!- The two activities are present on separate domains. -!- Formerly EC 3.1.4.15. P9WN39 P9WN39 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. P9WN40 P9WN40 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. P9WN41 P9WN41 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. P9WN47 P9WN47 2.1.1.44 L-histidine N(alpha)-methyltransferase. Dimethylhistidine N-methyltransferase. 3 S-adenosyl-L-methionine + L-histidine = 3 S-adenosyl-L-homocysteine + hercynine. -!- Part of the biosynthetic pathway of ergothioneine. P9WN51 P9WN51 2.1.2.10 Aminomethyltransferase. Glycine synthase. Glycine-cleavage system T-protein. Tetrahydrofolate aminomethyltransferase. [Protein]-S(8)-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH(3). -!- A component, with EC 1.4.4.2 and EC 1.8.1.4, of the glycine cleavage system, formerly known as glycine synthase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. P9WN83 P9WN83 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. P9WN93 P9WN93 4.2.1.2 Fumarate hydratase. Fumarase. (S)-malate = fumarate + H(2)O. P9WN97 P9WN97 2.4.1.129 Peptidoglycan glycosyltransferase. Bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)- pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D- glucosaminyltransferase. Penicillin binding protein (3 or 1B). Peptidoglycan TGase. Peptidoglycan transglycosylase. PG-II. (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)- diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala- gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate. -!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. -!- Involved in the synthesis of cell-wall peptidoglycan. P9WNE5 P9WNE5 1.16.3.1 Ferroxidase. Ceruloplasmin. HEPH. Hephaestin. 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. Cu cation. P9WNG2 P9WNG2 2.3.1.180 Beta-ketoacyl-[acyl-carrier-protein] synthase III. 3-ketoacyl-acyl carrier protein synthase III. 3-oxoacyl:ACP synthase III. Beta-ketoacyl (acyl carrier protein) synthase III. Beta-ketoacyl-ACP synthase III. Beta-ketoacyl-acyl carrier protein synthase III. KAS III. KASIII. Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier- protein] + CoA + CO(2). -!- Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer. -!- In addition to the above reaction, the enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent. -!- Responsible for initiating both straight- and branched-chain fatty- acid biosynthesis, with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism. -!- For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight- and branched-chain (C4--C6) acyl-CoA primers whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA. P9WNG3 P9WNG3 2.3.1.180 Beta-ketoacyl-[acyl-carrier-protein] synthase III. 3-ketoacyl-acyl carrier protein synthase III. 3-oxoacyl:ACP synthase III. Beta-ketoacyl (acyl carrier protein) synthase III. Beta-ketoacyl-ACP synthase III. Beta-ketoacyl-acyl carrier protein synthase III. KAS III. KASIII. Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier- protein] + CoA + CO(2). -!- Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer. -!- In addition to the above reaction, the enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent. -!- Responsible for initiating both straight- and branched-chain fatty- acid biosynthesis, with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism. -!- For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight- and branched-chain (C4--C6) acyl-CoA primers whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA. P9WNH1 P9WNH1 1.11.1.18 Bromide peroxidase. Bromoperoxidase. Eosinophil peroxidase. RH + HBr + H(2)O(2) = RBr + 2 H(2)O. -!- Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate. -!- They catalyze the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds. -!- Bromoperoxidases also oxidize iodides. P9WNH5 P9WNH5 3.7.1.8 2,6-dioxo-6-phenylhexa-3-enoate hydrolase. HOHPDA hydrolase. 2,6-dioxo-6-phenylhexa-3-enoate + H(2)O = benzoate + 2-oxopent-4-enoate. -!- Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 by ring-fission at a -CO-C bond. -!- Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp. P9WNH5 P9WNH5 3.7.1.17 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase. (1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4- oate + H(2)O = 3-((3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4- yl)propanoate + (2Z,4Z)-2-hydroxyhexa-2,4-dienoate. -!- The enzyme is involved in the bacterial degradation of the steroid ring structure, and is involved in degradation of multiple steroids, such as testosterone, cholesterol, and sitosterol. P9WNM5 P9WNM5 2.7.1.25 Adenylyl-sulfate kinase. Adenosine 5'-phosphosulfate kinase. Adenylylsulfate kinase. APS kinase. ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate. -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. P9WNM5 P9WNM5 2.7.7.4 Sulfate adenylyltransferase. ATP-sulfurylase. Sulfate adenylate transferase. Sulfurylase. ATP + sulfate = diphosphate + adenylyl sulfate. -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. P9WNN7 P9WNN7 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). P9WNN9 P9WNN9 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). P9WNP1 P9WNP1 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). P9WNP5 P9WNP5 4.1.3.36 1,4-dihydroxy-2-naphthoyl-CoA synthase. DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing). 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O. -!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzyme A group is subsequently removed from the product by EC 3.1.2.28. P9WNU7 P9WNU7 6.3.1.19 Prokaryotic ubiquitin-like protein ligase. Proteasome accessory factor A. Pup ligase. Pup--protein ligase. Pup-conjugating enzyme. ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L- lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-like protein]- gamma-L-glutamyl)-[protein]-L-lysine. -!- The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum. -!- It catalyzes the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an epsilon-amino group of a lysine residue of the target protein and the gamma- carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup). -!- The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation. -!- Formerly EC 6.3.2.n2. P9WNV1 P9WNV1 6.5.1.2 DNA ligase (NAD(+)). DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (NAD(+)). Polydeoxyribonucleotide synthase (NAD+). Polynucleotide ligase (NAD(+)). Polynucleotide ligase (NAD+). NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide. -!- The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7. P9WNV3 P9WNV3 6.5.1.1 DNA ligase (ATP). DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (ATP). Polynucleotide ligase (ATP). Sealase. ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate. -!- The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7. P9WNV5 P9WNV5 6.5.1.1 DNA ligase (ATP). DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (ATP). Polynucleotide ligase (ATP). Sealase. ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate. -!- The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7. P9WNX2 P9WNX2 1.1.1.95 Phosphoglycerate dehydrogenase. 3-phosphoglycerate dehydrogenase. 3-phosphoglyceric acid dehydrogenase. 3PHP reductase. Alpha-KG reductase. Alpha-phosphoglycerate dehydrogenase. D-3-phosphoglycerate dehydrogenase. Glycerate 3-phosphate dehydrogenase. Glycerate-1,3-phosphate dehydrogenase. PGDH. Phosphoglycerate oxidoreductase. Phosphoglyceric acid dehydrogenase. 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. -!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399. P9WNX2 P9WNX2 1.1.1.399 2-oxoglutarate reductase. (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. -!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95. P9WNX3 P9WNX3 1.1.1.95 Phosphoglycerate dehydrogenase. 3-phosphoglycerate dehydrogenase. 3-phosphoglyceric acid dehydrogenase. 3PHP reductase. Alpha-KG reductase. Alpha-phosphoglycerate dehydrogenase. D-3-phosphoglycerate dehydrogenase. Glycerate 3-phosphate dehydrogenase. Glycerate-1,3-phosphate dehydrogenase. PGDH. Phosphoglycerate oxidoreductase. Phosphoglyceric acid dehydrogenase. 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. -!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399. P9WNX3 P9WNX3 1.1.1.399 2-oxoglutarate reductase. (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. -!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95. P9WNY0 P9WNY0 1.2.1.3 Aldehyde dehydrogenase (NAD(+)). An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH. -!- Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. -!- Formerly EC 1.1.1.70. P9WNY1 P9WNY1 1.2.1.3 Aldehyde dehydrogenase (NAD(+)). An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH. -!- Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. -!- Formerly EC 1.1.1.70. P9WNZ0 P9WNZ0 4.1.1.36 Phosphopantothenoylcysteine decarboxylase. N-((R)-4'-phosphopantothenoyl)-L-cysteine carboxy-lyase. N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO(2). FMN. P9WNZ0 P9WNZ0 6.3.2.5 Phosphopantothenate--cysteine ligase (CTP). Phosphopantothenate--cysteine ligase. Phosphopantothenoylcysteine synthetase. CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine. P9WNZ1 P9WNZ1 4.1.1.36 Phosphopantothenoylcysteine decarboxylase. N-((R)-4'-phosphopantothenoyl)-L-cysteine carboxy-lyase. N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO(2). FMN. P9WNZ1 P9WNZ1 6.3.2.5 Phosphopantothenate--cysteine ligase (CTP). Phosphopantothenate--cysteine ligase. Phosphopantothenoylcysteine synthetase. CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine. P9WP37 P9WP37 7.1.1.8 Quinol--cytochrome-c reductase. Complex III (mitochondrial electron transport). Cytochrome bc1 complex. Ubiquinol--cytochrome-c reductase. Ubiquinone--cytochrome-c oxidoreductase. Quinol + 2 ferricytochrome c(Side 2) = quinone + 2 ferrocytochrome c(Side 2) + 2 H(+)(Side 2). -!- The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. -!- It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. -!- The mammalian enzyme contains cytochromes b-562, b-566 and c(1), and a 2-iron ferredoxin. -!- Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non- cytoplasmic compartment (cf. EC 1.6.99.3). -!- Formerly EC 1.10.2.2. P9WP65 P9WP65 3.1.4.53 3',5'-cyclic-AMP phosphodiesterase. cAMP-specific PDE. cAMP-specific phosphodiesterase. Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate. -!- Specific for 3',5'-cAMP and does not hydrolyze other nucleoside 3',5'-cyclic phosphates such as cGMP (cf. EC 3.1.4.17 and EC 3.1.4.35). -!- It is involved in modulation of the levels of cAMP, which is a mediator in the processes of cell transformation and proliferation. -!- Formerly EC 3.1.4.n1. P9WP67 P9WP67 1.9.3.1 Cytochrome-c oxidase. Complex IV (mitochondrial electron transport). Cytochrome a3. Cytochrome aa3. Cytochrome oxidase. Warburg's respiratory enzyme. 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. Cu cation. -!- The reduction of O(2) to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. -!- Several bacteria appear to contain analogous oxidases. P9WP71 P9WP71 1.9.3.1 Cytochrome-c oxidase. Complex IV (mitochondrial electron transport). Cytochrome a3. Cytochrome aa3. Cytochrome oxidase. Warburg's respiratory enzyme. 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. Cu cation. -!- The reduction of O(2) to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. -!- Several bacteria appear to contain analogous oxidases. P9WP77 P9WP77 2.5.1.147 5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase. 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine. Iron-sulfur. -!- The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy- 5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. -!- FO is also produced by some cyanobacteria and eukaryotes. -!- The enzyme, which forms a complex with EC 4.3.1.32 is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to initiate the reaction. -!- Formerly EC 2.5.1.77. P9WP77 P9WP77 4.3.1.32 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. F(0)-synthase. FO synthase. 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH(3) + L-methionine + 5'-deoxyadenosine. -!- The enzyme produces the F(0) precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. -!- F(0) is also produced by some cyanobacteria and eukaryotes. -!- The enzyme, which forms a complex with EC 2.5.1.147, is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to catalyze the condensation reaction. -!- Formerly EC 2.5.1.77. P9WPA2 P9WPA2 2.7.1.24 Dephospho-CoA kinase. Dephosphocoenzyme A kinase. ATP + 3'-dephospho-CoA = ADP + CoA. P9WPA3 P9WPA3 2.7.1.24 Dephospho-CoA kinase. Dephosphocoenzyme A kinase. ATP + 3'-dephospho-CoA = ADP + CoA. P9WPB3 P9WPB3 2.1.1.79 Cyclopropane-fatty-acyl-phospholipid synthase. CFA synthase. Cyclopropane fatty acid synthase. Cyclopropane synthetase. Unsaturated-phospholipid methyltransferase. S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl- L-homocysteine + phospholipid cyclopropane fatty acid. -!- Adds a methylene group across the 9,10 position of a Delta(9)- olefinic acyl chain in phosphatidylethanolamine or, more slowly, phosphatidylglycerol or phosphatidylinositol forming a cyclopropane derivative (cf. EC 2.1.1.16). P9WPB5 P9WPB5 2.1.1.79 Cyclopropane-fatty-acyl-phospholipid synthase. CFA synthase. Cyclopropane fatty acid synthase. Cyclopropane synthetase. Unsaturated-phospholipid methyltransferase. S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl- L-homocysteine + phospholipid cyclopropane fatty acid. -!- Adds a methylene group across the 9,10 position of a Delta(9)- olefinic acyl chain in phosphatidylethanolamine or, more slowly, phosphatidylglycerol or phosphatidylinositol forming a cyclopropane derivative (cf. EC 2.1.1.16). P9WPC4 P9WPC4 3.4.21.92 Endopeptidase Clp. Caseinolytic protease. Endopeptidase Ti. Protease Ti. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). -!- Belongs to peptidase family S14. P9WPC5 P9WPC5 3.4.21.92 Endopeptidase Clp. Caseinolytic protease. Endopeptidase Ti. Protease Ti. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). -!- Belongs to peptidase family S14. P9WPD4 P9WPD4 2.3.3.16 Citrate synthase (unknown stereospecificity). Citrate condensing enzyme. Citrate synthetase. Citric synthase. Citric-condensing enzyme. Citrogenase. CoA-acetylating citrate oxaloacetate-lyase. Condensing enzyme. Oxalacetic transacetase. Oxaloacetate transacetase. Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. -!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3). P9WPD5 P9WPD5 2.3.3.16 Citrate synthase (unknown stereospecificity). Citrate condensing enzyme. Citrate synthetase. Citric synthase. Citric-condensing enzyme. Citrogenase. CoA-acetylating citrate oxaloacetate-lyase. Condensing enzyme. Oxalacetic transacetase. Oxaloacetate transacetase. Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. -!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3). P9WPQ3 P9WPQ3 6.3.4.14 Biotin carboxylase. ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]- carboxybiotin-N(6)-L-lysine. -!- This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15. -!- In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). -!- Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyzes the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2). P9WPQ7 P9WPQ7 2.8.1.6 Biotin synthase. Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin. Iron-sulfur. -!- The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster. -!- In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and a putative dethiobiotinyl carbon radical. -!- Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring. -!- The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover. -!- In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis. P9WPS2 P9WPS2 7.2.2.8 P-type Cu(+) transporter. Cu(+)-exporting ATPase. ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2). -!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- This enzyme transports Cu(+) or Ag(+), and cannot transport the divalent ions, contrary to EC 7.2.2.9, which mainly transports the divalent copper ion. -!- Formerly EC 3.6.3.54. P9WPS3 P9WPS3 7.2.2.8 P-type Cu(+) transporter. Cu(+)-exporting ATPase. ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2). -!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- This enzyme transports Cu(+) or Ag(+), and cannot transport the divalent ions, contrary to EC 7.2.2.9, which mainly transports the divalent copper ion. -!- Formerly EC 3.6.3.54. P9WPU1 P9WPU1 7.2.2.8 P-type Cu(+) transporter. Cu(+)-exporting ATPase. ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2). -!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- This enzyme transports Cu(+) or Ag(+), and cannot transport the divalent ions, contrary to EC 7.2.2.9, which mainly transports the divalent copper ion. -!- Formerly EC 3.6.3.54. P9WPU5 P9WPU5 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. P9WPW7 P9WPW7 6.3.4.5 Argininosuccinate synthase. Arginine succinate synthetase. Argininosuccinate synthetase. Citrulline--aspartate ligase. ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate. P9WPX3 P9WPX3 2.7.2.4 Aspartate kinase. Aspartokinase. ATP + L-aspartate = ADP + 4-phospho-L-aspartate. -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3. -!- This is also the case for two of the four isoenzymes in Arabidopsis thaliana. -!- The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction. P9WPZ3 P9WPZ3 2.3.1.1 Amino-acid N-acetyltransferase. N-acetylglutamate synthase. Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. -!- Also acts with L-aspartate and, more slowly, with some other amino acids. P9WPZ3 P9WPZ3 2.3.1.35 Glutamate N-acetyltransferase. Acetylglutamate synthetase. Acetylglutamate-acetylornithine transacetylase. Acetylglutamic synthetase. Acetylglutamic-acetylornithine transacetylase. Acetylornithinase. Acetylornithine glutamate acetyltransferase. Glutamate acetyltransferase. N-acetyl-L-glutamate synthetase. N-acetylglutamate synthase. N-acetylglutamate synthetase. Ornithine acetyltransferase. Ornithine transacetylase. N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L- glutamate. -!- Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity. P9WQ01 P9WQ01 2.7.2.8 Acetylglutamate kinase. ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. P9WQ17 P9WQ17 2.4.99.16 Starch synthase (maltosyl-transferring). Alpha-1,4-glucan:maltose-1-P maltosyltransferase. GMPMT. Alpha-maltose 1-phosphate + ((1->4)-alpha-D-glucosyl)(n) = phosphate + ((1->4)-alpha-D-glucosyl)(n+2). -!- The enzyme from from the bacterium Mycobacterium smegmatis is specific for maltose. -!- It has no activity with alpha-D-glucose. -!- Formerly EC 2.4.1.n5. P9WQ27 P9WQ27 2.4.1.18 1,4-alpha-glucan branching enzyme. Amylo-(1,4 to 1,6)transglucosidase. Amylo-(1,4->1,6)-transglycosylase. Branching enzyme. Glycogen branching enzyme. Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. -!- Converts amylose into amylopectin. -!- The description (official name) requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. -!- The latter has frequently been termed Q-enzyme. P9WQ61 P9WQ61 6.2.1.50 4-hydroxybenzoate adenylyltransferase FadD22. 4-hydroxybenzoate adenylase. ATP + 4-hydroxybenzoate + holo-[4-hydroxyphenylalkanoate synthase] = AMP + diphosphate + 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase]. -!- This mycobacterial enzyme participates in the biosynthesis of phenolphthiocerols. -!- Following the substrate's activation by adenylation, it is transferred to an acyl-carrier protein domain within the enzyme, from which it is transferred to EC 2.3.1.261. -!- Formerly EC 2.7.7.98. P9WQ71 P9WQ71 2.8.1.7 Cysteine desulfurase. Cysteine desulfurylase. L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. Pyridoxal 5'-phosphate. -!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. P9WQ97 P9WQ97 3.5.1.4 Amidase. Acylamidase. Acylase. A monocarboxylic acid amide + H(2)O = a monocarboxylate + NH(3). P9WQ99 P9WQ99 3.5.1.4 Amidase. Acylamidase. Acylase. A monocarboxylic acid amide + H(2)O = a monocarboxylate + NH(3). P9WQA3 P9WQA3 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. P9WQB3 P9WQB3 2.3.3.13 2-isopropylmalate synthase. 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating). Alpha-IPM synthetase. Alpha-isopropylmalate synthase. Alpha-isopropylmalate synthetase. Alpha-isopropylmalic synthetase. Isopropylmalate synthase. Isopropylmalate synthetase. Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA. K(+). -!- Formerly EC 4.1.3.12. P9WQD7 P9WQD7 2.3.1.41 Beta-ketoacyl-[acyl-carrier-protein] synthase I. 3-ketoacyl-acyl carrier protein synthase. 3-oxoacyl-[acyl-carrier-protein] synthase. Acyl-malonyl acyl carrier protein-condensing enzyme. Acyl-malonyl(acyl-carrier-protein)-condensing enzyme. Beta-ketoacyl acyl carrier protein synthase. Beta-ketoacyl synthetase. Beta-ketoacyl-[acyl carrier protein] synthase. Beta-ketoacyl-ACP synthase I. Beta-ketoacyl-ACP synthetase. Beta-ketoacyl-acyl carrier protein synthetase. Beta-ketoacylsynthase. Condensing enzyme. Fatty acid condensing enzyme. KAS I. Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. -!- Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. -!- Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature. P9WQH1 P9WQH1 2.7.2.1 Acetate kinase. Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK. ATP + acetate = ADP + acetyl phosphate. Mg(2+). -!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. P9WQH7 P9WQH7 6.4.1.3 Propionyl-CoA carboxylase. PCCase. ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl- CoA. Biotin. -!- Also carboxylates butanoyl-CoA and catalyzes transcarboxylation. P9WQK9 P9WQK9 7.3.2.1 ABC-type phosphate transporter. ABC phosphate transporter. Phosphate-transporting ATPase. ATP + H(2)O + phosphate-[phosphate-binding protein](Side 1) = ADP + phosphate + phosphate(Side 2) + [phosphate-binding protein](Side 1). -!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of phosphate anions. -!- Unlike P-type ATPases, it does not undergo phosphorylation during the transport process. -!- Formerly EC 3.6.3.27. P9WQN9 P9WQN9 2.3.1.20 Diacylglycerol O-acyltransferase. Diglyceride acyltransferase. Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. -!- Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. P9WQN9 P9WQN9 2.3.1.122 Trehalose O-mycolyltransferase. 2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose + alpha,alpha'-trehalose 6,6'-bismycolate. -!- Catalyzes the exchange of mycolic acid between trehalose, trehalose mycolate and trehalose bismycolate. -!- Trehalose 6-palmitate can also act as donor. Q01462 Q01462 1.1.1.27 L-lactate dehydrogenase. L-lactic acid dehydrogenase. L-lactic dehydrogenase. (S)-lactate + NAD(+) = pyruvate + NADH. -!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme. Q02E25 Q02E25 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q02E40 Q02E40 5.4.2.2 Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent). Glucose phosphomutase. Phosphoglucose mutase. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. -!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1. Q02E40 Q02E40 5.4.2.8 Phosphomannomutase. Phosphomannose mutase. Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. -!- Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.7. Q02I31 Q02I31 4.2.1.96 4a-hydroxytetrahydrobiopterin dehydratase. 4-alpha-hydroxy-tetrahydropterin dehydratase. Pterin-4-alpha-carbinolamine dehydratase. Tetrahydrobiopterin dehydratase. (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro- 4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro- 6H-pterin + H(2)O. -!- Catalyzes the dehydration of 4a-hydroxytetrahydrobiopterins. Q02K73 Q02K73 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. Q02K94 Q02K94 2.3.1.41 Beta-ketoacyl-[acyl-carrier-protein] synthase I. 3-ketoacyl-acyl carrier protein synthase. 3-oxoacyl-[acyl-carrier-protein] synthase. Acyl-malonyl acyl carrier protein-condensing enzyme. Acyl-malonyl(acyl-carrier-protein)-condensing enzyme. Beta-ketoacyl acyl carrier protein synthase. Beta-ketoacyl synthetase. Beta-ketoacyl-[acyl carrier protein] synthase. Beta-ketoacyl-ACP synthase I. Beta-ketoacyl-ACP synthetase. Beta-ketoacyl-acyl carrier protein synthetase. Beta-ketoacylsynthase. Condensing enzyme. Fatty acid condensing enzyme. KAS I. Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. -!- Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. -!- Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature. Q02KR1 Q02KR1 2.7.9.2 Pyruvate, water dikinase. Phosphoenolpyruvate synthase. Pyruvate,water dikinase. ATP + pyruvate + H(2)O = AMP + phosphoenolpyruvate + phosphate. Mn(2+). Q02KR3 Q02KR3 4.1.1.112 Oxaloacetate decarboxylase. Oxalate beta-decarboxylase. Oxaloacetate carboxy-lyase. Oxaloacetate = pyruvate + CO(2). -!- The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn(2+), while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg(2+). -!- Unlike EC 7.2.4.2, there is no evidence of the enzyme's involvement in Na(+) transport. -!- Formerly EC 4.1.1.3. Q02KR3 Q02KR3 4.1.3.17 4-hydroxy-4-methyl-2-oxoglutarate aldolase. 4-carboxy-4-hydroxy-2-oxoadipate aldolase. 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase. CHA aldolase. HMG aldolase. (1) 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate. (2) 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate. Divalent cation. -!- This enzyme participates in the degradation of protocatechuate (via the meta-cleavage pathway), phthalate, syringate and gallate. -!- The enzyme from Pseudomonas ochraceae can also cleave 4-hydroxy-2- oxoglutarate to glyoxylate and pyruvate, and also catalyzes the reaction of EC 4.1.1.3. Q02KT5 Q02KT5 6.1.1.18 Glutamine--tRNA ligase. Glutamine translase. Glutaminyl-tRNA synthetase. ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl- tRNA(Gln). Q02NB5 Q02NB5 1.1.1.42 Isocitrate dehydrogenase (NADP(+)). Dual-cofactor-specific isocitrate dehydrogenase. IDH. IDP. Isocitrate (NADP) dehydrogenase. Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Isocitrate dehydrogenase (NADP). Isocitrate dehydrogenase (NADP-dependent). NADP isocitric dehydrogenase. NADP(+)-ICDH. NADP(+)-IDH. NADP(+)-linked isocitrate dehydrogenase. NADP-dependent isocitrate dehydrogenase. NADP-dependent isocitric dehydrogenase. NADP-linked isocitrate dehydrogenase. NADP-specific isocitrate dehydrogenase. Oxalosuccinate decarboxylase. Oxalsuccinic decarboxylase. Triphosphopyridine nucleotide-linked isocitrate dehydrogenase- oxalosuccinate carboxylase. Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Mn(2+) or Mg(2+). -!- Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate. -!- In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. -!- The enzyme from some species can also use NAD(+) but much more slowly. Q02PA2 Q02PA2 3.4.11.1 Leucyl aminopeptidase. Cytosol aminopeptidase. Leucine aminopeptidase. Peptidase S. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Zn(2+). -!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC 3.4.1.1. Q02PH8 Q02PH8 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase. Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase. (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. -!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211). Q02PH8 Q02PH8 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). Q02PH8 Q02PH8 5.1.2.3 3-hydroxybutyryl-CoA epimerase. (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. Q02PH8 Q02PH8 5.3.3.8 Delta(3)-Delta(2)-enoyl-CoA isomerase. 3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase. (1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. -!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters. Q02QC9 Q02QC9 3.1.3.1 Alkaline phosphatase. Alkaline phosphomonoesterase. Glycerophosphatase. Phosphomonoesterase. A phosphate monoester + H(2)O = an alcohol + phosphate. Mg(2+); Zn(2+). -!- Active at a high pH optimum. -!- Wide specificity. -!- Also catalyzes transphosphorylations. -!- Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1). Q02RA7 Q02RA7 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. Q02RJ6 Q02RJ6 3.4.24.26 Pseudolysin. Pseudomonas aeruginosa neutral metalloproteinase. Pseudomonas elastase. Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects. Ca(2+); Zn(2+). -!- Causes tissue damage. -!- Belongs to peptidase family M4. -!- Formerly EC 3.4.24.4. Q02SM0 Q02SM0 2.5.1.78 6,7-dimethyl-8-ribityllumazine synthase. Lumazine synthase. 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6- (D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H(2)O + phosphate. -!- Involved in riboflavin biosynthesis. Q02SZ7 Q02SZ7 3.4.21.50 Lysyl endopeptidase. Achromobacter proteinase I. Lysyl bond specific proteinase. Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro. -!- Isolated from Achromobacter lyticus. -!- Enzymes with similar specificity are produced by Lysobacter enzymogenes (endoproteinase Lys-C) and Pseudomonas aeruginosa (Ps-1). -!- Belongs to peptidase family S1. Q02TI3 Q02TI3 2.3.1.234 N(6)-L-threonylcarbamoyladenine synthase. T6A synthase. L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N(6)-L- threonylcarbamoyladenine(37) in tRNA. -!- The enzyme is involved in the synthesis of N(6)- threonylcarbamoyladenosine(37) in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNA(Ile), tRNA(Thr), tRNA(Asn), tRNA(Lys), tRNA(Ser) and tRNA(Arg). -!- Formerly EC 2.6.99.4. Q02UU0 Q02UU0 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. Q04797 Q04797 1.2.1.11 Aspartate-semialdehyde dehydrogenase. ASA dehydrogenase. Aspartic semialdehyde dehydrogenase. L-aspartate-beta-semialdehyde dehydrogenase. L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH. Q04DH2 Q04DH2 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. Q04FD8 Q04FD8 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). Q04G20 Q04G20 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q04I74 Q04I74 6.1.1.1 Tyrosine--tRNA ligase. L-tyrosine-tRNA(Tyr) ligase (AMP-forming). Tyrosine translase. Tyrosine tRNA synthetase. Tyrosine-transfer ribonucleate synthetase. Tyrosine-transfer RNA ligase. Tyrosyl-transfer ribonucleate synthetase. Tyrosyl-transfer ribonucleic acid synthetase. Tyrosyl-transfer RNA synthetase. Tyrosyl-tRNA ligase. Tyrosyl-tRNA synthetase. ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). Q04IK6 Q04IK6 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q04IK7 Q04IK7 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q04J43 Q04J43 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. Q04JB0 Q04JB0 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q04JP7 Q04JP7 3.5.1.88 Peptide deformylase. PDF. Polypeptide deformylase. Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide. Fe(2+). -!- Requires at least a dipeptide for an efficient rate of reaction. -!- N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. -!- Differs in substrate specificity from EC 3.5.1.27 and EC 3.5.1.31. Q04JW5 Q04JW5 6.1.1.7 Alanine--tRNA ligase. Alanine translase. Alanyl-tRNA synthetase. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). Q04K99 Q04K99 1.1.1.27 L-lactate dehydrogenase. L-lactic acid dehydrogenase. L-lactic dehydrogenase. (S)-lactate + NAD(+) = pyruvate + NADH. -!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme. Q04KL8 Q04KL8 4.1.1.31 Phosphoenolpyruvate carboxylase. PEP carboxylase. PEPCase. Phosphoenolpyruvic carboxylase. Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-). -!- This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. -!- The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate. Q04KU2 Q04KU2 2.3.1.157 Glucosamine-1-phosphate N-acetyltransferase. Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate. -!- The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23. Q04KU2 Q04KU2 2.7.7.23 UDP-N-acetylglucosamine diphosphorylase. N-acetylglucosamine-1-phosphate uridyltransferase. UDP-N-acetylglucosamine pyrophosphorylase. UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine. -!- Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. -!- The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. -!- The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate. Q04KU8 Q04KU8 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. Q04L24 Q04L24 2.7.1.11 6-phosphofructokinase. Phosphofructokinase I. Phosphohexokinase. ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. -!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. -!- UTP, CTP and ITP can act as donors. -!- Not identical with EC 2.7.1.105. Q04LE0 Q04LE0 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. Q04LI2 Q04LI2 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). Q04LU1 Q04LU1 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). Q04LZ5 Q04LZ5 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. Q04M41 Q04M41 6.3.5.7 Glutaminyl-tRNA synthase (glutamine-hydrolyzing). GatCAB. GatDE. GatFAB. Glu-AdT. Glu-tRNA(Gln) amidotransferase. Glutamyl-tRNA(Gln) amidotransferase. ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. -!- In systems lacking discernible glutamine--tRNA ligase (EC 6.1.1.18), glutaminyl-tRNA(Gln) is formed by a two-enzyme system. -!- In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln). -!- The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl- tRNA(Glu) is not a substrate for this enzyme). -!- A glutaminase subunit (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. -!- Some bacterial GatCAB complexes also has the activity of EC 6.3.5.6. Q04ML1 Q04ML1 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q04ML5 Q04ML5 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. Q04N48 Q04N48 6.3.4.4 Adenylosuccinate synthase. Adenylosuccinate synthetase. IMP--aspartate ligase. Succinoadenylic kinosynthetase. GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)- AMP. Q05852 Q05852 2.7.7.9 UTP--glucose-1-phosphate uridylyltransferase. Glucose-1-phosphate uridylyltransferase. UDP-glucose diphosphorylase. UDP-glucose pyrophosphorylase. UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose. Q05873 Q05873 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q06067 Q06067 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. Q06473 Q06473 1.9.3.1 Cytochrome-c oxidase. Complex IV (mitochondrial electron transport). Cytochrome a3. Cytochrome aa3. Cytochrome oxidase. Warburg's respiratory enzyme. 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. Cu cation. -!- The reduction of O(2) to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. -!- Several bacteria appear to contain analogous oxidases. Q06752 Q06752 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). Q07635 Q07635 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. Q08582 Q08582 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). Q08582 Q08582 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. Q0P8U6 Q0P8U6 2.7.7.81 Pseudaminic acid cytidylyltransferase. CTP + 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-2- nonulopyranosonic acid = diphosphate + CMP-5,7-diacetamido-3,5,7,9- tetradeoxy-L-glycero-alpha-L-manno-2-nonulopyranosonic acid. Mg(2+). Q0PA50 Q0PA50 3.1.3.11 Fructose-bisphosphatase. Fructose 1,6-bisphosphatase. Hexose diphosphatase. D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. -!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. Q2FX12 Q2FX12 3.1.3.48 Protein-tyrosine-phosphatase. Phosphotyrosine phosphatase. PTPase. Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. -!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2. Q3K0T0 Q3K0T0 2.7.10.2 Non-specific protein-tyrosine kinase. Cytoplasmic protein tyrosine kinase. ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. -!- Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain. -!- In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families. -!- Formerly EC 2.7.1.112. Q3K1F5 Q3K1F5 1.8.4.12 Peptide-methionine (R)-S-oxide reductase. Methionine S-oxide reductase. Methionine S-oxide reductase (R-form oxidizing). Methionine sulfoxide reductase. Methionine sulfoxide reductase B. Selenoprotein R. Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (R)-S-oxide + thioredoxin. Se(2+); Zn(2+). -!- The reaction occurs in the reverse direction to that shown above. -!- Exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide. -!- While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater. -!- Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. -!- The reaction proceeds via a sulfenic-acid intermediate. -!- For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well. Q3K1H1 Q3K1H1 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. Q3K1J7 Q3K1J7 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q3K2M3 Q3K2M3 3.1.11.6 Exodeoxyribonuclease VII. E.coli exonuclease VII. Exonuclease VII. Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates. -!- Preference for single-stranded DNA. -!- Similar enzyme: Micrococcus luteus exonuclease. Q3K2S4 Q3K2S4 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q3K3G5 Q3K3G5 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). Q3K6L5 Q3K6L5 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q3K7B6 Q3K7B6 1.17.7.3 (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin). (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase. (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H(2)O + oxidized flavodoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin. -!- Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria. -!- Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1). Q3KHL4 Q3KHL4 6.3.5.3 Phosphoribosylformylglycinamidine synthase. FGAM synthase. FGAM synthetase. FGAR amidotransferase. FGARAT. Formylglycinamide ribotide amidotransferase. Phosphoribosylformylglycinamidine synthetase. ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine + L-glutamate. Q3V5W6 Q3V5W6 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. Q44176 Q44176 4.1.1.39 Ribulose-bisphosphate carboxylase. Carboxydismutase. D-ribulose 1,5-diphosphate carboxylase. D-ribulose-1,5-bisphosphate carboxylase. Diphosphoribulose carboxylase. Ribulose 1,5-bisphosphate carboxylase. Ribulose 1,5-bisphosphate carboxylase/oxygenase. Ribulose 1,5-diphosphate carboxylase. Ribulose 1,5-diphosphate carboxylase/oxygenase. Ribulose bisphosphate carboxylase/oxygenase. Ribulose diphosphate carboxylase. Ribulose diphosphate carboxylase/oxygenase. RuBisCO. RuBP carboxylase. 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O. -!- Will utilize O(2) instead of CO(2), forming 3-phospho-D-glycerate and 2-phosphoglycolate. Q45477 Q45477 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q45495 Q45495 3.5.1.88 Peptide deformylase. PDF. Polypeptide deformylase. Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide. Fe(2+). -!- Requires at least a dipeptide for an efficient rate of reaction. -!- N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. -!- Differs in substrate specificity from EC 3.5.1.27 and EC 3.5.1.31. Q45499 Q45499 3.1.3.25 Inositol-phosphate phosphatase. Inositol 1-phosphatase. Inositol monophosphate phosphatase. Inositol phosphatase. Inositol-1(or 4)-monophosphatase. L-myo-inositol-1-phosphate phosphatase. Myo-inositol 1-phosphatase. Myo-inositol monophosphatase. Myo-inositol-1(or 4)-monophosphatase. Myo-inositol-1(or 4)-phosphate phosphohydrolase. Myo-inositol-1-phosphatase. Myo-inositol phosphate + H(2)O = myo-inositol + phosphate. -!- Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. -!- It also acts on adenosine 2'-phosphate (but not the 3'- or 5'-phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate, but does not act on inositol bisphosphates or more phosphorylated inositols. Q45582 Q45582 4.2.1.126 N-acetylmuramic acid 6-phosphate etherase. MurNAc-6-P etherase. (R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H(2)O. -!- This enzyme, along with EC 2.7.1.170, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. -!- The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling. -!- Formerly EC 4.2.1.n1. Q45614 Q45614 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. Q45829 Q45829 2.7.2.7 Butyrate kinase. ATP + butanoate = ADP + butanoyl phosphate. -!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14). Q46106 Q46106 1.16.3.2 Bacterial non-heme ferritin. 4 Fe(2+) + O(2) + 6 H(2)O = 4 (FeO(OH)) + 8 H(+). -!- Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life. -!- They are formed from two subunits that co-assemble in various ratios to form a spherical protein shell. -!- Thousands of mineralized iron atoms are stored within the core of the structure. -!- The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction. Q46920 Q46920 1.7.1.13 PreQ(1) synthase. 7-cyano-7-deazaguanine reductase. PreQ(0) oxidoreductase. PreQ(0) reductase. 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-carbaguanine + 2 NADPH. -!- The reaction occurs in the reverse direction. -!- This enzyme catalyzes one of the early steps in the synthesis of queosine (Q-tRNA), and is followed by the action of EC 2.4.2.29. -!- Queosine is found in the wobble position of tRNA(GUN) in eukaryotes and bacteria and is thought to be involved in translational modulation. Q47690 Q47690 2.1.1.10 Homocysteine S-methyltransferase. S-methyl-L-methionine + L-homocysteine = 2 L-methionine. -!- The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine. Q48662 Q48662 4.1.1.101 Malolactic enzyme. (S)-malate = (S)-lactate + CO(2). Mn(2+); NAD(+). -!- The enzyme is involved in the malolactic fermentation of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. -!- It has been purified from several lactic acid bacteria, including Leuconostoc mesenteroides, Lactobacillus plantarum, and Oenococcus oeni. Q48793 Q48793 2.7.6.1 Ribose-phosphate diphosphokinase. Phosphoribosyl diphosphate synthetase. Phosphoribosyl pyrophosphate synthetase. Ribose-phosphate pyrophosphokinase. ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. -!- dATP can also act as donor. Q4J6G3 Q4J6G3 2.8.1.4 tRNA uracil 4-sulfurtransferase. tRNA sulfurtransferase. ATP + [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-sulfur] cluster. -!- The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide. -!- The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP. -!- The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA. -!- The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes. Q4J6M3 Q4J6M3 1.2.99.8 Glyceraldehyde dehydrogenase (FAD-containing). Glyceraldehyde oxidoreductase. D-glyceraldehyde + H(2)O + acceptor = D-glycerate + reduced acceptor. FAD; Iron-sulfur; Molybdopterin guanine dinucleotide. -!- The enzyme from the archaeon Sulfolobus acidocaldarius catalyzes the oxidation of D-glyceraldehyde in the nonphosphorylative Entner- Doudoroff pathway. -!- With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde. -!- It is not known which acceptor is utilized in vivo. Q4J6M6 Q4J6M6 1.2.99.8 Glyceraldehyde dehydrogenase (FAD-containing). Glyceraldehyde oxidoreductase. D-glyceraldehyde + H(2)O + acceptor = D-glycerate + reduced acceptor. FAD; Iron-sulfur; Molybdopterin guanine dinucleotide. -!- The enzyme from the archaeon Sulfolobus acidocaldarius catalyzes the oxidation of D-glyceraldehyde in the nonphosphorylative Entner- Doudoroff pathway. -!- With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde. -!- It is not known which acceptor is utilized in vivo. Q4J6Z4 Q4J6Z4 1.18.1.2 Ferredoxin--NADP(+) reductase. 2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH. FAD. -!- In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin. -!- Formerly EC 1.6.7.1 and EC 1.6.99.4. Q4J7A3 Q4J7A3 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. Q4J860 Q4J860 4.2.1.9 Dihydroxy-acid dehydratase. 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H(2)O. Q4J8E8 Q4J8E8 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. Q4J8F1 Q4J8F1 6.3.4.5 Argininosuccinate synthase. Arginine succinate synthetase. Argininosuccinate synthetase. Citrulline--aspartate ligase. ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate. Q4J8F8 Q4J8F8 6.3.5.3 Phosphoribosylformylglycinamidine synthase. FGAM synthase. FGAM synthetase. FGAR amidotransferase. FGARAT. Formylglycinamide ribotide amidotransferase. Phosphoribosylformylglycinamidine synthetase. ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine + L-glutamate. Q4J8G0 Q4J8G0 6.3.2.6 Phosphoribosylaminoimidazolesuccinocarboxamide synthase. 4-((N-succinylamino)carbonyl)-5-aminoimidazole ribonucleotide synthetase. 4-(N-succinocarboxamide)-5-aminoimidazole synthetase. 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase. Phosphoribosylaminoimidazole-succinocarboxamide synthase. Phosphoribosylaminoimidazole-succinocarboxamide synthetase. Phosphoribosylaminoimidazolesuccinocarboxamide synthetase. SAICAR synthase. SAICAR synthetase. SAICARs. ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate. -!- Forms part of the purine biosynthesis pathway. Q4J8I4 Q4J8I4 6.1.1.11 Serine--tRNA ligase. Serine translase. SerRS. Seryl-transfer ribonucleate synthetase. Seryl-transfer ribonucleic acid synthetase. Seryl-transfer RNA synthetase. Seryl-tRNA synthetase. (1) ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). (2) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). -!- This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1. Q4J8I9 Q4J8I9 4.3.2.10 Imidazole glycerol-phosphate synthase. IGP synthase. 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho- beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1- (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1- (imidazol-4-yl)glycerol 3-phosphate + L-glutamate. -!- The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. -!- The enzymes from archaea and bacteria are heterodimeric. -!- A glutaminase component (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. -!- The glutminase subunit is only active within the dimeric complex. -!- In fungi and plants the two subunits are combined into a single polypeptide. Q4J8J2 Q4J8J2 2.4.2.17 ATP phosphoribosyltransferase. Phosphoribosyl-ATP diphosphorylase. Phosphoribosyl-ATP pyrophosphorylase. 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D- ribose 1-diphosphate. -!- Involved in histidine biosynthesis. Q4J8J7 Q4J8J7 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). Q4J8K9 Q4J8K9 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. Q4J8L2 Q4J8L2 3.5.1.2 Glutaminase. L-glutamine amidohydrolase. L-glutamine + H(2)O = L-glutamate + NH(3). Q4J8L2 Q4J8L2 4.3.3.6 Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing). D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate. -!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants. Q4J8L3 Q4J8L3 4.3.3.6 Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing). D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate. -!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants. Q4J8L4 Q4J8L4 6.1.1.15 Proline--tRNA ligase. Proline translase. Prolyl-tRNA synthetase. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). Q4J8P9 Q4J8P9 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). Q4J8Q0 Q4J8Q0 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). Q4J8T0 Q4J8T0 4.1.99.22 GTP 3',8-cyclase. GTP + S-adenosyl-L-methionine + reduced electron acceptor = (8S)-3',8- cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor. Iron-sulfur; S-adenosyl-L-methionine. -!- The enzyme catalyzes an early step in the biosynthesis of the molybdenum cofactor (MoCo). -!- The enzyme belongs to the superfamily of radical S-adenosyl-L- methionine (radical SAM) enzymes. -!- Formerly EC 4.1.99.18. Q4J8X8 Q4J8X8 4.2.1.20 Tryptophan synthase. Indoleglycerol phosphate aldolase. L-tryptophan synthetase. Tryptophan desmolase. Tryptophan synthetase. L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. Pyridoxal 5'-phosphate. -!- The alpha-subunit catalyzes the conversion of 1-C-(indol-3- yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8). -!- The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. -!- In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24. -!- In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). -!- That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex. Q4J8X9 Q4J8X9 3.6.1.7 Acylphosphatase. Acylphosphate phosphohydrolase. An acylphosphate + H(2)O = a carboxylate + phosphate. Q4J904 Q4J904 6.1.1.19 Arginine--tRNA ligase. Arginine translase. Arginyl-tRNA synthetase. ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). Q4J915 Q4J915 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. Q4J929 Q4J929 4.2.99.18 DNA-(apurinic or apyrimidinic site) lyase. AP endonuclease class I. AP lyase. Deoxyribonuclease (apurinic or apyrimidinic). E.coli endonuclease III. Endodeoxyribonuclease (apurinic or apyrimidinic). Micrococcus luteus UV endonuclease. Phage-T(4) UV endonuclease. Phage-T4 UV endonuclease. The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. -!- 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. -!- This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2. Q4J939 Q4J939 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. Q4J940 Q4J940 1.2.1.59 Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating). NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase (NAD(P)(+)). Triosephosphate dehydrogenase (NAD(P)). D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D- glyceroyl phosphate + NAD(P)H. -!- NAD(+) and NADP(+) can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 and EC 1.2.1.13, which are NAD(+)- and NADP(+)- dependent, respectively. Q4J947 Q4J947 2.1.1.216 tRNA (guanine(26)-N(2))-dimethyltransferase. tRNA (m(2)(2)G(26))dimethyltransferase. 2 S-adenosyl-L-methionine + guanine(26) in tRNA = 2 S-adenosyl-L- homocysteine + N(2)-dimethylguanine(26) in tRNA. -!- The enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions. -!- In contrast to EC 2.1.1.215, this enzyme does not catalyze the methylation of guanine(27) in tRNA. -!- Formerly EC 2.1.1.32. Q4J978 Q4J978 2.5.1.46 Deoxyhypusine synthase. (4-aminobutyl)lysine synthase. [eIF-5A]-deoxyhypusine synthase. Spermidine dehydrogenase. [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine. NAD(+). -!- The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. -!- Catalyzes the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. -!- The reaction occurs in four steps: NAD(+)-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). -!- Hence the overall reaction is transfer of a 4-aminobutyl group. -!- For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. -!- Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29. -!- Formerly EC 1.1.1.249. Q4J986 Q4J986 2.7.4.22 UMP kinase. UMP-kinase. UMPK. Uridine monophosphate kinase. Uridylate kinase. ATP + UMP = ADP + UDP. -!- Strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme EC 2.7.4.14 for the same purpose. -!- Subject of feedback regulation, being inhibited by UTP and activated by GTP. Q4J9A0 Q4J9A0 2.7.7.72 CCA tRNA nucleotidyltransferase. CCA-adding enzyme. Ribonucleic cytidylic cytidylic adenylic pyrophosphorylase. Transfer ribonucleic adenylyl (cytidylyl) transferase. Transfer RNA adenylyltransferase. Transfer-RNA nucleotidyltransferase. tRNA adenylyl(cytidylyl)transferase. tRNA CCA-diphosphorylase. tRNA cytidylyltransferase. tRNA-nucleotidyltransferase. A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. -!- The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. -!- The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. -!- Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition. -!- Formerly EC 2.7.7.21 and EC 2.7.7.25. Q4J9C4 Q4J9C4 6.1.1.3 Threonine--tRNA ligase. Threonine translase. Threonyl-tRNA synthetase. ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). Q4J9C6 Q4J9C6 2.1.1.63 Methylated-DNA--[protein]-cysteine S-methyltransferase. 6-O-methylguanine-DNA methyltransferase. O-6-methylguanine-DNA-alkyltransferase. (1) DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine. (2) DNA (containing 4-O-methylthymine) + protein L-cysteine = DNA (without 4-O-methylthymine) + protein S-methyl-L-cysteine. -!- This protein is involved in the repair of methylated DNA. -!- Unlike EC 3.2.2.20 and EC 3.2.2.21, which remove the methylated base leaving an apurinic/apyrimidinic site, this enzyme transfers the methyl group from the methylated DNA to an internal cysteine residue, leaving an intact nucleotide. -!- Since the methyl transfer is irreversible, the enzyme can only catalyze a single turnover. Q4J9S8 Q4J9S8 4.1.1.32 Phosphoenolpyruvate carboxykinase (GTP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2). -!- ITP can act as phosphate donor. Q4JA60 Q4JA60 3.1.26.4 Ribonuclease H. Endoribonuclease H. RNase H. Endonucleolytic cleavage to 5'-phosphomonoester. -!- Acts on RNA-DNA hybrids. Q4JAA8 Q4JAA8 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. Q4JAB2 Q4JAB2 4.6.1.17 Cyclic pyranopterin monophosphate synthase. (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate. -!- The enzyme catalyzes an early step in the biosynthesis of the molybdenum cofactor (MoCo). -!- Formerly EC 4.1.99.18. Q4JAE8 Q4JAE8 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q4JAI7 Q4JAI7 6.3.5.11 Cobyrinate a,c-diamide synthase (glutamine-hydrolyzing). Cobyrinic acid a,c-diamide synthetase. 2 ATP + cobyrinate + 2 L-glutamine + 2 H(2)O = 2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate. -!- This enzyme is the first glutamine amidotransferase that participates in the anaerobic (early cobalt insertion) biosynthetic pathway of adenosylcobalamin, and catalyzes the ATP-dependent synthesis of cobyrinate a,c-diamide from cobyrinate using either L-glutamine or ammonia as the nitrogen source. -!- It is proposed that the enzyme first catalyzes the amidation of the c-carboxylate, and then the intermediate is released into solution and binds to the same catalytic site for the amidation of the a-carboxylate. -!- The Km for ammonia is substantially higher than that for L-glutamine. Q4JAJ2 Q4JAJ2 2.5.1.78 6,7-dimethyl-8-ribityllumazine synthase. Lumazine synthase. 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6- (D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H(2)O + phosphate. -!- Involved in riboflavin biosynthesis. Q4JAK8 Q4JAK8 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. Q4JAL1 Q4JAL1 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. Q4JAM7 Q4JAM7 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. Q4JAM9 Q4JAM9 1.2.1.70 Glutamyl-tRNA reductase. L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. -!- Forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway, which is used in most eubacteria, and in all archaebacteria, algae and plants. -!- However, in the alpha-proteobacteria EC 2.3.1.37 is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. -!- This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. -!- Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. Q4JAS3 Q4JAS3 2.5.1.41 Phosphoglycerol geranylgeranyltransferase. (S)-3-O-geranylgeranylglyceryl phosphate synthase. GGGP synthase. GGGPS. Geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate. Mg(2+). -!- Catalyzes the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria. -!- It catalyzes the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate. -!- The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 1.1.1.261, EC 2.5.1.42 and EC 2.7.7.67, which lead to the formation of CDP-unsaturated archaeol. -!- The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine. Q4JAT0 Q4JAT0 2.7.7.1 Nicotinamide-nucleotide adenylyltransferase. Adenosine triphosphate-nicotinamide mononucleotide transadenylase. Diphosphopyridine nucleotide pyrophosphorylase. NAD(+) diphosphorylase. NAD(+) pyrophosphorylase. Nicotinamide adenine dinucleotide pyrophosphorylase. Nicotinamide mononucleotide adenylyltransferase. NMN adenylyltransferase. NMNAT. ATP + nicotinamide ribonucleotide = diphosphate + NAD(+). -!- Nicotinate nucleotide can also act as acceptor. -!- See also EC 2.7.7.18. Q4JAU3 Q4JAU3 6.3.4.23 Formate--phosphoribosylaminoimidazolecarboxamide ligase. 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase. 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase. ATP + formate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = ADP + phosphate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide. -!- This archaeal enzyme, characterized from the methanogen Methanocaldococcus jannaschii, catalyzes a step in the synthesis of purine nucleotides. -!- It differs from the orthologous bacterial/eukaryotic enzymes, which utilize 10-formyltetrahydrofolate rather than formate and ATP. -!- Cf. EC 2.1.2.3. Q4JAY3 Q4JAY3 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. Q4JAZ7 Q4JAZ7 3.3.1.1 Adenosylhomocysteinase. Adenosylhomocysteine hydrolase. AdoHcyase. S-adenosylhomocysteinase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine synthase. SAHase. S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine. NAD(+). -!- The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4. Q4JAZ8 Q4JAZ8 2.5.1.16 Spermidine synthase. Aminopropyltransferase. Putrescine aminopropyltransferase. S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl- 5'-thioadenosine + spermidine. -!- The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor. -!- The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant toward other amine acceptors, such as spermidine and cadaverine. -!- Cf. EC 2.5.1.22 and EC 2.5.1.23. Q4JB01 Q4JB01 1.1.1.261 sn-glycerol-1-phosphate dehydrogenase. Glycerol-1-phosphate dehydrogenase (NAD(P)(+)). Gro1PDH. sn-glycerol 1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H. Zn(2+) or Ni(2+). -!- Responsible for the formation of archaea-specific sn-glycerol-1- phosphate, the first step in the biosynthesis of polar lipids in archaea. -!- It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. -!- The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 and EC 2.5.1.42, which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP- unsaturated archaeol. -!- The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine. -!- Activity of the enzyme is stimulated by K(+). Q4JB24 Q4JB24 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. Q4JB80 Q4JB80 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. Q4JBG0 Q4JBG0 2.3.1.255 N-terminal amino-acid N(alpha)-acetyltransferase NatA. (1) Acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-N(alpha)- acetyl-glycyl-[protein] + CoA. (2) Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal- N(alpha)-acetyl-L-alanyl-[protein] + CoA. (3) Acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal- N(alpha)-acetyl-L-seryl-[protein] + CoA. (4) Acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal- N(alpha)-acetyl-L-valyl-[protein] + CoA. (5) Acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal- N(alpha)-acetyl-L-cysteinyl-[protein] + CoA. (6) Acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal- N(alpha)-acetyl-L-threonyl-[protein] + CoA. -!- N-terminal-acetylases (NATs) catalyze the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. -!- This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. -!- The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine. -!- Formerly EC 2.3.1.88. Q4JBG0 Q4JBG0 2.3.1.258 N-terminal methionine N(alpha)-acetyltransferase NatE. (1) Acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-alanyl-[protein] + CoA. (2) Acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-seryl-[protein] + CoA. (3) Acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-valyl-[protein] + CoA. (4) Acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-threonyl-[protein] + CoA. (5) Acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-lysyl-[protein] + CoA. (6) Acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA. (7) Acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA. (8) Acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA. -!- N-terminal-acetylases (NATs) catalyze the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. -!- This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. -!- It may also play a role in membrane targeting and gene silencing. -!- NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. -!- It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. -!- There is some substrate overlap with EC 2.3.1.256. -!- In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18. -!- The enzyme also has the activity of EC 2.3.1.48 and autoacetylates several of its own lysine residues. -!- Formerly EC 2.3.1.88. Q4JBL7 Q4JBL7 2.1.1.196 Cobalt-precorrin-6B (C(15))-methyltransferase (decarboxylating). Cobalt-precorrin-6Y (C(15))-methyltransferase (decarboxylating). Cobalt-precorrin-6B + S-adenosyl-L-methionine = cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO(2). -!- This enzyme catalyzes both methylation at C-15 and decarboxylation of the C-12 acetate side chain of cobalt-precorrin-6B, a step in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway. Q4JBP0 Q4JBP0 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). Q4JBW3 Q4JBW3 2.7.7.1 Nicotinamide-nucleotide adenylyltransferase. Adenosine triphosphate-nicotinamide mononucleotide transadenylase. Diphosphopyridine nucleotide pyrophosphorylase. NAD(+) diphosphorylase. NAD(+) pyrophosphorylase. Nicotinamide adenine dinucleotide pyrophosphorylase. Nicotinamide mononucleotide adenylyltransferase. NMN adenylyltransferase. NMNAT. ATP + nicotinamide ribonucleotide = diphosphate + NAD(+). -!- Nicotinate nucleotide can also act as acceptor. -!- See also EC 2.7.7.18. Q4JC00 Q4JC00 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). Q4JC09 Q4JC09 4.2.1.33 3-isopropylmalate dehydratase. (2R,3S)-3-isopropylmalate hydro-lyase. 3-isopropylmalate hydro-lyase. Alpha-IPM isomerase. Isopropylmalate isomerase. (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. Iron-sulfur. -!- Forms part of the leucine-biosynthesis pathway. -!- Brings about the interconversion of the two isomers of isopropylmalate. Q4JC68 Q4JC68 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). Q4JCA6 Q4JCA6 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). Q4JCI5 Q4JCI5 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). Q4JCJ1 Q4JCJ1 4.1.1.31 Phosphoenolpyruvate carboxylase. PEP carboxylase. PEPCase. Phosphoenolpyruvic carboxylase. Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-). -!- This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. -!- The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate. Q4JCK7 Q4JCK7 3.1.1.96 D-aminoacyl-tRNA deacylase. D-tyr-tRNA(Tyr) deacylase. D-tyrosyl-tRNA(Tyr) aminoacylhydrolase. A D-aminoacyl-tRNA + H(2)O = a D-amino acid + tRNA. Zn(2+). -!- The enzyme from Escherichia coli can cleave D-tyrosyl-tRNA(Tyr), D-aspartyl-tRNA(Asp) and D-tryptophanyl-tRNA(Trp). -!- Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc. Q4JCL6 Q4JCL6 3.1.26.5 Ribonuclease P. Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. -!- Essential for tRNA processing; generates 5'-termini of mature tRNA molecules. Q50331 Q50331 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q51567 Q51567 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. Q54735 Q54735 4.2.1.1 Carbonic anhydrase. Carbonate dehydratase. Carbonate hydro-lyase. Carbonic dehydratase. H(2)CO(3) = CO(2) + H(2)O. Zn(2+). -!- The enzyme catalyzes the reversible hydration of gaseous CO(2) to carbonic acid, which spontaneously converts to hydrogencarbonate under neutral pH. -!- It is widespread and found in archaea, bacteria, and eukaryotes. -!- Three distinct classes exist, and appear to have evolved independently. Q55080 Q55080 1.11.1.7 Peroxidase. Lactoperoxidase. 2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O. Heme. Q55118 Q55118 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. Q55158 Q55158 1.1.1.193 5-amino-6-(5-phosphoribosylamino)uracil reductase. 5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6- (5-phospho-D-ribosylamino)uracil + NADPH. Q55158 Q55158 3.5.4.26 Diaminohydroxyphosphoribosylaminopyrimidine deaminase. 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5-phosphoribosylamino)uracil + NH(3). -!- The substrate is the product of EC 3.5.4.25. Q55168 Q55168 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. Q55318 Q55318 1.18.1.2 Ferredoxin--NADP(+) reductase. 2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH. FAD. -!- In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin. -!- Formerly EC 1.6.7.1 and EC 1.6.99.4. Q55338 Q55338 2.1.3.2 Aspartate carbamoyltransferase. Aspartate transcarbamylase. ATCase. Carbamylaspartotranskinase. Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. Q55404 Q55404 6.2.1.1 Acetate--CoA ligase. Acetate thiokinase. Acetyl-activating enzyme. Acetyl-CoA synthase. Acetyl-CoA synthetase. Acyl-activating enzyme. ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. -!- Also acts on propanoate and propenoate. Q55418 Q55418 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). Q55498 Q55498 5.4.99.18 5-(carboxyamino)imidazole ribonucleotide mutase. N(5)-CAIR mutase. N(5)-carboxyaminoimidazole ribonucleotide mutase. 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate. -!- In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates. -!- In the absence of EC 6.3.2.6, the reaction is reversible. -!- The substrate is readily converted into 5-amino-1-(5-phospho-D- ribosyl)imidazole by non-enzymic decarboxylation. Q55504 Q55504 2.3.1.157 Glucosamine-1-phosphate N-acetyltransferase. Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate. -!- The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23. Q55504 Q55504 2.7.7.23 UDP-N-acetylglucosamine diphosphorylase. N-acetylglucosamine-1-phosphate uridyltransferase. UDP-N-acetylglucosamine pyrophosphorylase. UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine. -!- Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. -!- The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. -!- The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate. Q55512 Q55512 1.2.1.11 Aspartate-semialdehyde dehydrogenase. ASA dehydrogenase. Aspartic semialdehyde dehydrogenase. L-aspartate-beta-semialdehyde dehydrogenase. L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH. Q55522 Q55522 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q55574 Q55574 2.4.2.10 Orotate phosphoribosyltransferase. OPRT. Orotidine-5'-phosphate diphosphorylase. Orotidine-5'-phosphate pyrophosphorylase. Orotidylic acid phosphorylase. Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. -!- The enzyme from higher eukaryotes also catalyzes the reaction listed as EC 4.1.1.23. Q55607 Q55607 1.3.7.7 Ferredoxin:protochlorophyllide reductase (ATP-dependent). Light-independent protochlorophyllide reductase. Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate. Iron-sulfur. -!- Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. -!- The enzyme catalyzes trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. -!- Unlike EC 1.3.1.33 light is not required. -!- The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of EC 1.18.6.1, which catalyzes an ATP-driven reduction. Q55664 Q55664 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. Q55665 Q55665 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. Q55729 Q55729 6.1.1.10 Methionine--tRNA ligase. Methionine translase. Methionyl-transfer ribonucleate synthetase. Methionyl-transfer ribonucleic acid synthetase. Methionyl-transfer RNA synthetase. Methionyl-tRNA synthetase. MetRS. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl- tRNA(Met). -!- In those organisms producing N-formylmethionyl-tRNA(fMet) for translation initiation, this enzyme also recognizes the initiator tRNA(fMet) and catalyzes the formation of L-methionyl-tRNA(fMet), the substrate for EC 2.1.2.9. Q55746 Q55746 2.3.1.129 Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase. Acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase. UDP-N-acetylglucosamine acyltransferase. (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D- glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)- N-acetyl-alpha-D-glucosamine. -!- Involved with EC 2.4.1.182 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli. Q55756 Q55756 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. Q55759 Q55759 3.5.4.16 GTP cyclohydrolase I. GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate. -!- The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. -!- Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12. Q55848 Q55848 2.7.6.1 Ribose-phosphate diphosphokinase. Phosphoribosyl diphosphate synthetase. Phosphoribosyl pyrophosphate synthetase. Ribose-phosphate pyrophosphokinase. ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. -!- dATP can also act as donor. Q55905 Q55905 2.7.9.2 Pyruvate, water dikinase. Phosphoenolpyruvate synthase. Pyruvate,water dikinase. ATP + pyruvate + H(2)O = AMP + phosphoenolpyruvate + phosphate. Mn(2+). Q55982 Q55982 1.1.1.262 4-hydroxythreonine-4-phosphate dehydrogenase. 4-(phosphohydroxy)-L-threonine dehydrogenase. L-threonine 4-phosphate dehydrogenase. NAD(+)-dependent threonine 4-phosphate dehydrogenase. 4-phosphooxy-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO(2) + NADH. -!- The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria. Q56582 Q56582 7.2.1.1 NADH:ubiquinone reductase (Na(+)-transporting). Na(+)-NQR. Na(+)-translocating NADH-quinone reductase. NADH + ubiquinone + n Na(+)(In) = NAD(+) + ubiquinol + n Na(+)(Out). FAD; FMN; Iron-sulfur; Riboflavin. -!- An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster. -!- Formerly EC 1.6.5.8. Q56584 Q56584 7.2.1.1 NADH:ubiquinone reductase (Na(+)-transporting). Na(+)-NQR. Na(+)-translocating NADH-quinone reductase. NADH + ubiquinone + n Na(+)(In) = NAD(+) + ubiquinol + n Na(+)(Out). FAD; FMN; Iron-sulfur; Riboflavin. -!- An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster. -!- Formerly EC 1.6.5.8. Q56587 Q56587 7.2.1.1 NADH:ubiquinone reductase (Na(+)-transporting). Na(+)-NQR. Na(+)-translocating NADH-quinone reductase. NADH + ubiquinone + n Na(+)(In) = NAD(+) + ubiquinol + n Na(+)(Out). FAD; FMN; Iron-sulfur; Riboflavin. -!- An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster. -!- Formerly EC 1.6.5.8. Q57QC4 Q57QC4 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. Q59641 Q59641 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. Q59969 Q59969 6.3.5.5 Carbamoyl-phosphate synthase (glutamine-hydrolyzing). Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. Q59992 Q59992 4.2.1.20 Tryptophan synthase. Indoleglycerol phosphate aldolase. L-tryptophan synthetase. Tryptophan desmolase. Tryptophan synthetase. L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. Pyridoxal 5'-phosphate. -!- The alpha-subunit catalyzes the conversion of 1-C-(indol-3- yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8). -!- The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. -!- In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24. -!- In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). -!- That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex. Q59993 Q59993 3.4.21.92 Endopeptidase Clp. Caseinolytic protease. Endopeptidase Ti. Protease Ti. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). -!- Belongs to peptidase family S14. Q5HCU6 Q5HCU6 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. Q5HCZ6 Q5HCZ6 1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenase. 1-pyrroline-5-carboxylate dehydrogenase. Delta(1)-pyrroline-5-carboxylate dehydrogenase. Pyrroline-5-carboxylate dehydrogenase. L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH. -!- This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. -!- (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. -!- In many bacterial species, both activities are carried out by a single bifunctional enzyme. -!- The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. -!- NADP(+) can also act as acceptor, but with lower activity. -!- Formerly EC 1.5.1.12. Q5HD61 Q5HD61 5.4.2.2 Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent). Glucose phosphomutase. Phosphoglucose mutase. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. -!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1. Q5HDX9 Q5HDX9 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. Q5HE43 Q5HE43 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. Q5HE73 Q5HE73 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. Q5HE75 Q5HE75 4.1.2.13 Fructose-bisphosphate aldolase. Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Zn(2+). -!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7. Q5HE87 Q5HE87 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. Q5HE88 Q5HE88 2.4.2.9 Uracil phosphoribosyltransferase. UMP diphosphorylase. UMP pyrophosphorylase. UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. Q5HE95 Q5HE95 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q5HEE0 Q5HEE0 4.3.1.19 Threonine ammonia-lyase. L-serine dehydratase. L-threonine deaminase. L-threonine dehydratase. L-threonine hydro-lyase (deaminating). Serine deaminase. Threonine deaminase. Threonine dehydrase. Threonine dehydratase. L-threonine = 2-oxobutanoate + NH(3). Pyridoxal 5'-phosphate or iron-sulfur. -!- The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond. -!- The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10. -!- The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17. -!- Formerly EC 4.2.1.16. Q5HEL4 Q5HEL4 4.3.2.2 Adenylosuccinate lyase. Adenylosuccinase. Succino AMP-lyase. (1) N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (2) (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide. -!- Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5- aminoimidazole. Q5HEL8 Q5HEL8 6.5.1.2 DNA ligase (NAD(+)). DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (NAD(+)). Polydeoxyribonucleotide synthase (NAD+). Polynucleotide ligase (NAD(+)). Polynucleotide ligase (NAD+). NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide. -!- The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7. Q5HEU2 Q5HEU2 4.1.1.37 Uroporphyrinogen decarboxylase. Uroporphyrinogen III decarboxylase. Uroporphyrinogen-III carboxy-lyase. Uroporphyrinogen III = coproporphyrinogen + 4 CO(2). -!- Acts on a number of porphyrinogens. Q5HF16 Q5HF16 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). Q5HF24 Q5HF24 2.6.1.21 D-amino-acid transaminase. D-alanine aminotransferase. D-alanine transaminase. D-alanine-D-glutamate transaminase. D-amino acid aminotransferase. D-amino acid transaminase. D-aspartate aminotransferase. D-aspartate transaminase. D-aspartic aminotransferase. D-alanine + 2-oxoglutarate = pyruvate + D-glutamate. Pyridoxal 5'-phosphate. -!- The enzyme from thermophilic Bacillus species acts on many D-amino acids with D-alanine and D-2-aminobutyrate as the best amino donors. -!- It can similarly use any of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and 2-oxobutyrate among the best. -!- The enzyme from some other sources has a broader specificity. -!- Formerly EC 2.6.1.10. Q5HF42 Q5HF42 6.3.4.3 Formate--tetrahydrofolate ligase. Formyltetrahydrofolate synthetase. Tetrahydrofolate formylase. Tetrahydrofolic formylase. ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. -!- In eukaryotes occurs as a trifunctional enzyme also having EC 1.5.1.5 and EC 3.5.4.9 activity. Q5HF73 Q5HF73 2.1.3.15 Acetyl-CoA carboxytransferase. [Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl- CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl- CoA. -!- The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. -!- In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2). -!- Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3). Q5HF76 Q5HF76 2.7.1.40 Pyruvate kinase. Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase. ATP + pyruvate = ADP + phosphoenolpyruvate. -!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). Q5HF90 Q5HF90 6.1.1.3 Threonine--tRNA ligase. Threonine translase. Threonyl-tRNA synthetase. ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). Q5HF97 Q5HF97 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. Q5HFA2 Q5HFA2 2.5.1.61 Hydroxymethylbilane synthase. (4-(2-carboxyethyl)-3-(carboxymethyl)pyrrol-2-yl)methyltransferase (hydrolyzing). HMB-synthase. Porphobilinogen deaminase. Pre-uroporphyrinogen synthase. Uroporphyrinogen I synthase. Uroporphyrinogen I synthetase. Uroporphyrinogen synthase. Uroporphyrinogen synthetase. 4 porphobilinogen + H(2)O = hydroxymethylbilane + 4 NH(3). Dipyrromethane. -!- The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active center. -!- The terminal tetrapyrrole is then hydrolyzed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. -!- In the presence of a second enzyme, EC 4.2.1.75, which is often called cosynthase, the product is cyclized to form uroporphyrinogen III. -!- If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I. -!- Formerly EC 4.3.1.8. Q5HFA4 Q5HFA4 4.2.1.24 Porphobilinogen synthase. Aminolevulinate dehydratase. Delta-aminolevulinic acid dehydratase. 2 5-aminolevulinate = porphobilinogen + 2 H(2)O. Zn(2+). -!- The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. -!- The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. -!- In humans, the enzyme is a primary target for the environmental toxin Pb. -!- The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation. Q5HFA8 Q5HFA8 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q5HFC4 Q5HFC4 2.4.2.29 tRNA-guanine(34) transglycosylase. Guanine insertion enzyme. Q-insertase. Queuine tRNA-ribosyltransferase. Queuine(34) transfer ribonucleate ribosyltransferase. TGT. tRNA guanine(34) transglycosidase. tRNA transglycosylase. (1) Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. (2) Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine(34) in tRNA + guanine. -!- Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. -!- In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. -!- In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ(1), which is ultimately modified to queuine. -!- The eubacterial enzyme can also use an earlier intermediate, preQ(0), to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn). -!- This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway. Q5HFC8 Q5HFC8 2.4.2.7 Adenine phosphoribosyltransferase. AMP diphosphorylase. AMP pyrophosphorylase. APRT. Transphosphoribosidase. AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. -!- 5-amino-4-imidazolecarboxamide can replace adenine. Q5HFJ5 Q5HFJ5 6.1.1.14 Glycine--tRNA ligase. Glycyl translase. Glycyl-tRNA synthetase. ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). Q5HFK3 Q5HFK3 3.1.21.2 Deoxyribonuclease IV. Deoxyribonuclease IV (phage T4-induced). Endodeoxyribonuclease IV (phage T(4)-induced). Endodeoxyribonuclease IV (phage T4-induced). Endonuclease II. Endonuclease IV. Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. -!- The enzyme is an apurinic/apyrimidinic (AP) site endonuclease that primes DNA repair synthesis at AP sites. -!- It specifically cleaves the DNA backbone at AP sites and also removes 3' DNA-blocking groups such as 3' phosphates, 3' phosphoglycolates, and 3' alpha,beta-unsaturated aldehydes that arise from oxidative base damage and the activity of combined glycosylase/lyase enzymes. -!- It is also the only known repair enzyme that is able to cleave the DNA backbone 5' of the oxidative lesion alpha-deoxyadenosine. -!- The enzyme has a strong preference for single-stranded DNA. -!- Formerly EC 3.1.4.30. Q5HFM3 Q5HFM3 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. Q5HFM4 Q5HFM4 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. Q5HFR2 Q5HFR2 1.1.1.44 Phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating). 6-phosphogluconic carboxylase. 6-phosphogluconic dehydrogenase. 6PGD. Phosphogluconic acid dehydrogenase. 6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH. -!- The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. -!- Highly specific for NADP(+). -!- Cf. EC 1.1.1.343. Q5HFV4 Q5HFV4 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. Q5HFV7 Q5HFV7 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. Q5HG06 Q5HG06 1.2.4.2 Oxoglutarate dehydrogenase (succinyl-transferring). 2-ketoglutarate dehydrogenase. 2-oxoglutarate dehydrogenase. 2-oxoglutarate: lipoate oxidoreductase. 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- succinylating). AKGDH. Alpha-ketoglutarate dehydrogenase. Alpha-ketoglutaric acid dehydrogenase. Alpha-ketoglutaric dehydrogenase. Alpha-oxoglutarate dehydrogenase. Ketoglutaric dehydrogenase. OGDC. Oxoglutarate decarboxylase. Oxoglutarate dehydrogenase. Oxoglutarate dehydrogenase (lipoamide). 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61. Q5HG07 Q5HG07 2.3.1.61 Dihydrolipoyllysine-residue succinyltransferase. Dihydrolipoamide S-succinyltransferase. Dihydrolipoamide succinyltransferase. Dihydrolipoic transsuccinylase. Dihydrolipolyl transsuccinylase. Dihydrolipoyl transsuccinylase. Lipoate succinyltransferase. Lipoic transsuccinylase. Lipoyl transsuccinylase. Succinyl-CoA:dihydrolipoamide S-succinyltransferase. Succinyl-CoA:dihydrolipoate S-succinyltransferase. Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine. -!- A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A. Q5HG66 Q5HG66 2.3.1.275 Acyl phosphate:glycerol-3-phosphate acyltransferase. Acyl-phosphate--glycerol-3-phosphate acyltransferase. Acyl-PO(4) G3P acyltransferase. G3P acyltransferase. Glycerol-3-phosphate acyltransferase (acyl-phosphate transferring). GPAT. LPA synthase. Lysophosphatidic acid synthase. An acyl-phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycerol 3-phosphate + phosphate. -!- The enzyme, found in bacteria, catalyzes a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. -!- The enzyme is membrane-bound. -!- Formerly EC 2.3.1.n3. Q5HG69 Q5HG69 4.2.1.3 Aconitate hydratase. Aconitase. Cis-aconitase. Citrate hydro-lyase. Citrate(isocitrate) hydro-lyase. Citrate = isocitrate. Iron-sulfur. -!- Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. -!- The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. -!- Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3- tricarboxylate. -!- Formerly EC 4.2.1.4. Q5HG69 Q5HG69 4.2.1.99 2-methylisocitrate dehydratase. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3- tricarboxylate + H(2)O. -!- The enzyme from the fungus Yarrowia lipolytica does not act on isocitrate. Q5HG77 Q5HG77 2.2.1.1 Transketolase. Glycoaldehyde transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. Thiamine diphosphate. -!- Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH. -!- The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor. Q5HG86 Q5HG86 1.11.1.6 Catalase. 2 H(2)O(2) = O(2) + 2 H(2)O. Heme; Mn(2+). -!- A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase. -!- The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. -!- Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21. Q5HGC3 Q5HGC3 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. Q5HGF7 Q5HGF7 2.7.7.8 Polyribonucleotide nucleotidyltransferase. Polynucleotide phosphorylase. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. -!- ADP, IDP, GDP, UDP and CDP can act as donors. Q5HGI6 Q5HGI6 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. Q5HGI7 Q5HGI7 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. Q5HGK2 Q5HGK2 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH. -!- Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates. Q5HGL4 Q5HGL4 2.1.1.192 23S rRNA (adenine(2503)-C(2))-methyltransferase. (1) 2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe- 2S] ferredoxin. (2) 2 S-adenosyl-L-methionine + adenine(37) in tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 oxidized [2Fe-2S] ferredoxin. Iron-sulfur. -!- This enzyme is a member of the 'AdoMet radical' (radical SAM) family. -!- S-adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group. -!- RlmN first transfers an CH(2) group to a conserved cysteine (Cys(355) in Escherichia coli), the generated radical from a second S-adenosyl- L-methionine then attacks the methyl group, exctracting a hydrogen. -!- The formed radical forms a covalent intermediate with the adenine group of the tRNA. -!- RlmN is an endogenous enzyme used by the cell to refine functions of the ribosome in protein synthesis. -!- The enzyme methylates adenosine by a radical mechanism with CH(2) from the S-adenosyl-L-methionine and retention of the hydrogen at C-2 of adenosine(2503) of 23S rRNA. -!- It will also methylate 8-methyladenosine(2503) of 23S rRNA (cf. EC 2.1.1.224). Q5HGN8 Q5HGN8 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q5HGP8 Q5HGP8 6.3.2.9 UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase. D-glutamate ligase. D-glutamate-adding enzyme. MurD synthetase. UDP-Mur-NAC-L-Ala:D-Glu ligase. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase. UDP-N-acetylmuramoylalanine--D-glutamate ligase. Uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase. ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate. -!- Involved in the synthesis of a cell-wall peptide in bacteria. Q5HGP9 Q5HGP9 2.7.8.13 Phospho-N-acetylmuramoyl-pentapeptide-transferase. MraY transferase. Phospho-MurNAc-pentapeptide transferase. Phospho-N-acetylmuramoyl pentapeptide translocase. Phospho-NAc-muramoyl-pentapeptide translocase (UMP). Phosphoacetylmuramoylpentapeptide translocase. Phosphoacetylmuramoylpentapeptidetransferase. UDP-MurNAc-Ala-gamma-DGlu-Lys-DAla-DAla:undecaprenylphosphate transferase. UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C(55)-isoprenoid alcohol transferase. UDP-MurNAc-pentapeptide phosphotransferase. UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- diphosphoundecaprenol. -!- In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-center. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. Q5HGY8 Q5HGY8 1.8.1.4 Dihydrolipoyl dehydrogenase. Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. FAD. -!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3. Q5HGY9 Q5HGY9 2.3.1.12 Dihydrolipoyllysine-residue acetyltransferase. Acetyl-CoA:dihydrolipoamide S-acetyltransferase. Dihydrolipoamide S-acetyltransferase. Dihydrolipoate acetyltransferase. Dihydrolipoic transacetylase. Dihydrolipoyl acetyltransferase. Lipoate acetyltransferase. Lipoate transacetylase. Lipoic acetyltransferase. Lipoic acid acetyltransferase. Lipoic transacetylase. Lipoylacetyltransferase. Thioltransacetylase A. Transacetylase X. Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine. -!- A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A. Q5HGZ0 Q5HGZ0 1.2.4.1 Pyruvate dehydrogenase (acetyl-transferring). MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase. Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. Q5HGZ1 Q5HGZ1 1.2.4.1 Pyruvate dehydrogenase (acetyl-transferring). MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase. Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). Thiamine diphosphate. -!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. Q5HH21 Q5HH21 1.5.1.5 Methylenetetrahydrofolate dehydrogenase (NADP(+)). 5,10-methylenetetrahydrofolate + NADP(+) = 5,10- methenyltetrahydrofolate + NADPH. Q5HH21 Q5HH21 3.5.4.9 Methenyltetrahydrofolate cyclohydrolase. 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate. Q5HH38 Q5HH38 4.1.3.36 1,4-dihydroxy-2-naphthoyl-CoA synthase. DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing). 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O. -!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzyme A group is subsequently removed from the product by EC 3.1.2.28. Q5HH78 Q5HH78 2.7.1.23 NAD(+) kinase. DPN kinase. ATP + NAD(+) = ADP + NADP(+). Q5HH88 Q5HH88 6.1.1.2 Tryptophan--tRNA ligase. L-tryptophan-tRNA(Trp) ligase (AMP-forming). TrpRS. Tryptophan translase. Tryptophanyl ribonucleic synthetase. Tryptophanyl-transfer ribonucleate synthetase. Tryptophanyl-transfer ribonucleic acid synthetase. Tryptophanyl-transfer ribonucleic synthetase. Tryptophanyl-transfer RNA synthetase. Tryptophanyl-tRNA synthase. Tryptophanyl-tRNA synthetase. ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl- tRNA(Trp). Q5HHA2 Q5HHA2 2.3.1.180 Beta-ketoacyl-[acyl-carrier-protein] synthase III. 3-ketoacyl-acyl carrier protein synthase III. 3-oxoacyl:ACP synthase III. Beta-ketoacyl (acyl carrier protein) synthase III. Beta-ketoacyl-ACP synthase III. Beta-ketoacyl-acyl carrier protein synthase III. KAS III. KASIII. Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier- protein] + CoA + CO(2). -!- Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer. -!- In addition to the above reaction, the enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent. -!- Responsible for initiating both straight- and branched-chain fatty- acid biosynthesis, with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism. -!- For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight- and branched-chain (C4--C6) acyl-CoA primers whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA. Q5HHC2 Q5HHC2 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. Q5HHC7 Q5HHC7 1.4.1.2 Glutamate dehydrogenase. Glutamic dehydrogenase. L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH. Q5HHG0 Q5HHG0 2.8.1.8 Lipoyl synthase. Lipoate synthase. [Protein]-N(6)-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S](2+) cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H(+) = [protein]-N(6)-((R)-dihydrolipoyl)-L- lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe(3+) + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin. Iron-sulfur. -!- This enzyme catalyzes the final step in the de novo biosynthesis of the lipoyl cofactor, the attachment of two sulfhydryl groups to C(6) and C(8) of a pendant octanoyl chain. -!- It is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (S-adenosylmethionine) by the addition of an electron from an iron-sulfur center. -!- The enzyme contains two [4Fe-4S] clusters. -!- The first cluster produces the radicals, which are converted into 5'-deoxyadenosine when they abstract hydrogen atoms from C(6) and C(8), respectively, leaving reactive radicals at these positions that interact with sulfur atoms within the second (auxiliary) cluster. -!- Having donated two sulfur atoms, the auxiliary cluster is degraded during catalysis, but is regenerated immediately by the transfer of a new cluster from iron-sulfur cluster carrier proteins. -!- Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. -!- Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). -!- An alternative lipoylation pathway involves EC 6.3.1.20, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs). Q5HHP1 Q5HHP1 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. Q5HHP3 Q5HHP3 5.3.1.1 Triose-phosphate isomerase. Phosphotriose isomerase. Triose phosphoisomerase. Triosephosphate isomerase. Triosephosphate mutase. D-glyceraldehyde 3-phosphate = glycerone phosphate. Q5HHP5 Q5HHP5 1.2.1.12 Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate. Q5HHS7 Q5HHS7 3.4.11.4 Tripeptide aminopeptidase. Aminoexotripeptidase. Aminotripeptidase. Imidoendopeptidase. Lymphopeptidase. Peptidase B. Tripeptidase. Release of the N-terminal residue from a tripeptide. Zn(2+). -!- Widely distributed in mammalian tissues. -!- Belongs to peptidase family M9. -!- Formerly EC 3.4.1.3. Q5HI88 Q5HI88 2.3.1.8 Phosphate acetyltransferase. Phosphoacylase. Phosphotransacetylase. Acetyl-CoA + phosphate = CoA + acetyl phosphate. -!- Also acts with other short-chain acyl-CoAs. Q5HIA5 Q5HIA5 4.1.2.43 3-hexulose-6-phosphate synthase. 3-hexulose phosphate synthase. 3-hexulosephosphate synthase. D-arabino-3-hexulose 6-phosphate formaldehyde-lyase. HPS. D-arabino-hex-3-ulose 6-phosphate = D-ribulose 5-phosphate + formaldehyde. Mn(2+) or Mg(2+). -!- Specific for formaldehyde and D-ribulose 5-phosphate as substrates. -!- Ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate. -!- This enzyme, along with EC 5.3.1.27, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds. -!- The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyzes the reactions of this enzyme and EC 5.3.1.27. Q5HID2 Q5HID2 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q5HID3 Q5HID3 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q5HIE7 Q5HIE7 6.1.1.17 Glutamate--tRNA ligase. Glutamic acid translase. Glutamyl-tRNA synthetase. ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). Q5HIF5 Q5HIF5 4.3.3.6 Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing). D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate. -!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants. Q5HIF7 Q5HIF7 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). Q5HIJ5 Q5HIJ5 2.7.4.9 dTMP kinase. Thymidylate kinase. Thymidylic acid kinase. TMPK. ATP + dTMP = ADP + dTDP. Q5HIQ7 Q5HIQ7 1.1.1.205 IMP dehydrogenase. IMP oxidoreductase. Inosinate dehydrogenase. Inosine 5'-monophosphate dehydrogenase. Inosine monophosphate oxidoreductase. Inosinic acid dehydrogenase. Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH. -!- The enzyme acts on the hydroxy group of the hydrated derivative of the substrate. -!- Formerly EC 1.2.1.14. Q5HIT8 Q5HIT8 2.1.1.14 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. Cobalamin-independent methionine synthase. Homocysteine methylase. Methionine synthase (cobalamin-independent). Methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase. Tetrahydropteroylglutamate-homocysteine transmethylase. 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. Zn(2+). -!- Requires phosphate. -!- The enzyme from Escherichia coli also requires a reducing system. -!- Unlike EC 2.1.1.13 this enzyme does not contain cobalamin. Q5HJM9 Q5HJM9 5.4.2.7 Phosphopentomutase. Deoxyribomutase. Deoxyribose phosphomutase. Phosphodeoxyribomutase. Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. -!- Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D- ribose 5-phosphate. -!- Alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5- bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.6. Q5HJZ0 Q5HJZ0 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. Q5SHQ9 Q5SHQ9 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. Q5SI56 Q5SI56 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. Q5SJ45 Q5SJ45 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q5SJ94 Q5SJ94 1.5.1.5 Methylenetetrahydrofolate dehydrogenase (NADP(+)). 5,10-methylenetetrahydrofolate + NADP(+) = 5,10- methenyltetrahydrofolate + NADPH. Q5SJ94 Q5SJ94 3.5.4.9 Methenyltetrahydrofolate cyclohydrolase. 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate. Q5SJB8 Q5SJB8 2.1.1.148 Thymidylate synthase (FAD). FDTS. Flavin dependent thymidylate synthase. 5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+). -!- Contains FAD. -!- All thymidylate synthases catalyze a reductive methylation involving the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5-position of dUMP and a two electron reduction of the methylene group to a methyl group. -!- Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses folate as both a 1-carbon donor and a source of reducing equivalents, this enzyme uses a flavin coenzyme as a source of reducing equivalents, which are derived from NADPH. Q5SJE8 Q5SJE8 2.2.1.2 Transaldolase. Dihydroxyacetone transferase. Glycerone transferase. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. Q5SKV7 Q5SKV7 1.1.1.37 Malate dehydrogenase. Malic dehydrogenase. (S)-malate + NAD(+) = oxaloacetate + NADH. -!- Also oxidizes some other 2-hydroxydicarboxylic acids. Q5SL35 Q5SL35 2.7.4.25 (d)CMP kinase. dCMP kinase. Deoxycytidine monophosphokinase. Deoxycytidylate kinase. ATP + (d)CMP = ADP + (d)CDP. -!- The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. -!- Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22. -!- The enzyme phosphorylates dCMP nearly as well as it does CMP. Q5SL36 Q5SL36 2.5.1.19 3-phosphoshikimate 1-carboxyvinyltransferase. 3-enol-pyruvoylshikimate-5-phosphate synthase. 5-enolpyruvylshikimate-3-phosphate synthase. EPSP synthase. Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate. Q5SM27 Q5SM27 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. Q6N5C3 Q6N5C3 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. Q6N693 Q6N693 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. Q6NCN8 Q6NCN8 2.7.7.8 Polyribonucleotide nucleotidyltransferase. Polynucleotide phosphorylase. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. -!- ADP, IDP, GDP, UDP and CDP can act as donors. Q6NCP1 Q6NCP1 1.11.1.21 Catalase peroxidase. (1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O. -!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. Q6NCX7 Q6NCX7 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. Q6RKB1 Q6RKB1 1.2.1.30 Carboxylate reductase (NADP(+)). Aryl-aldehyde dehydrogenase (NADP(+)). An aromatic aldehyde + NADP(+) + AMP + diphosphate = an aromatic acid + NADPH + ATP. -!- The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. -!- The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. -!- The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released. Q72GG0 Q72GG0 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. Q72GQ0 Q72GQ0 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. Q72GY7 Q72GY7 4.1.1.49 Phosphoenolpyruvate carboxykinase (ATP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2). Q72I53 Q72I53 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. Q72IN0 Q72IN0 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. Q72IW9 Q72IW9 1.1.1.87 Homoisocitrate dehydrogenase. (-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD(+) oxidoreductase (decarboxylating). 2-hydroxy-3-carboxyadipate dehydrogenase. 3-carboxy-2-hydroxyadipate dehydrogenase. 3-carboxy-2-hydroxyadipate:NAD(+) oxidoreductase (decarboxylating). Homoisocitric dehydrogenase. (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD(+) = 2-oxoadipate + CO(2) + NADH. -!- Forms part of the lysine biosynthesis pathway in fungi. -!- Formerly EC 1.1.1.155. Q72JG7 Q72JG7 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q72JN9 Q72JN9 2.1.1.148 Thymidylate synthase (FAD). FDTS. Flavin dependent thymidylate synthase. 5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+). -!- Contains FAD. -!- All thymidylate synthases catalyze a reductive methylation involving the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5-position of dUMP and a two electron reduction of the methylene group to a methyl group. -!- Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses folate as both a 1-carbon donor and a source of reducing equivalents, this enzyme uses a flavin coenzyme as a source of reducing equivalents, which are derived from NADPH. Q72JS7 Q72JS7 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. Q72LH0 Q72LH0 2.7.4.25 (d)CMP kinase. dCMP kinase. Deoxycytidine monophosphokinase. Deoxycytidylate kinase. ATP + (d)CMP = ADP + (d)CDP. -!- The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. -!- Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22. -!- The enzyme phosphorylates dCMP nearly as well as it does CMP. Q72LH1 Q72LH1 2.5.1.19 3-phosphoshikimate 1-carboxyvinyltransferase. 3-enol-pyruvoylshikimate-5-phosphate synthase. 5-enolpyruvylshikimate-3-phosphate synthase. EPSP synthase. Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate. Q79PF4 Q79PF4 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. Q7AKQ6 Q7AKQ6 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. Q7DBF3 Q7DBF3 2.6.1.102 GDP-perosamine synthase. GDP-4-keto-6-deoxy-D-mannose-4-aminotransferase. GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate = GDP-4-dehydro- 6-deoxy-alpha-D-mannose + L-glutamate. Pyridoxal 5'-phosphate. -!- D-perosamine is one of several dideoxy sugars found in the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria. -!- The enzyme catalyzes the final step in GDP-perosamine synthesis. Q7DDR9 Q7DDR9 2.7.7.n1 Protein adenylyltransferase. (1) ATP + [protein]-L-tyrosine = diphosphate + [protein]-O(4)- (5'-adenylyl)-L-tyrosine. (2) ATP + [protein]-L-threonine = diphosphate + [protein]-O(4)- (5'-adenylyl)-L-threonine. Q7LXU0 Q7LXU0 3.1.22.4 Crossover junction endodeoxyribonuclease. Crossover junction endoribonuclease. Cruciform-cutting endonuclease. Endo X3. Endonuclease RuvC. Endonuclease VII. Endonuclease X3. Hje endonuclease. Holliday junction endonuclease CCE1. Holliday junction nuclease. Holliday junction resolvase. Holliday junction-cleaving endonuclease. Holliday junction-resolving endoribonuclease. Resolving enzyme CCE1. RusA endonuclease. RusA Holliday junction resolvase. RuvC endonuclease. SpCCe1 Holliday junction resolvase. Endonucleolytic cleavage at a junction such as a reciprocal single- stranded crossover between two homologous DNA duplexes (Holliday junction). -!- The enzyme from Saccharomyces cerevisiae has no endonuclease or exonuclease activity on single-stranded or double-stranded DNA molecules that do not contain Holliday junctions. Q7LYI9 Q7LYI9 1.1.1.47 Glucose 1-dehydrogenase (NAD(P)(+)). D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H. -!- This enzyme has similar activity with either NAD(+) or NADP(+). -!- Cf. EC 1.1.1.118 and EC 1.1.1.119. Q7MI93 Q7MI93 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. Q7MP86 Q7MP86 2.1.1.182 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase. 4 S-adenosyl-L-methionine + adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(1518)/N(6)- dimethyladenine(1519) in 16S rRNA. -!- KsgA introduces the most highly conserved ribosomal RNA modification, the dimethylation of adenine(1518) and adenine(1519) in 16S rRNA. -!- Strains lacking the methylase are resistant to kasugamycin. -!- Formerly EC 2.1.1.48. Q7TZN1 Q7TZN1 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. Q7UAE6 Q7UAE6 6.1.1.12 Aspartate--tRNA ligase. Aspartic acid translase. Aspartyl-tRNA synthetase. ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). Q7UAH4 Q7UAH4 2.8.1.7 Cysteine desulfurase. Cysteine desulfurylase. L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. Pyridoxal 5'-phosphate. -!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. Q7UAH4 Q7UAH4 4.4.1.16 Selenocysteine lyase. Selenocysteine beta-lyase. Selenocysteine reductase. L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor. Pyridoxal 5'-phosphate. -!- Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. -!- The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7). Q7UAV7 Q7UAV7 2.1.1.242 16S rRNA (guanine(1516)-N(2))-methyltransferase. M(2)G(1516) methyltransferase. S-adenosyl-L-methionine + guanine(1516) in 16S rRNA = S-adenosyl-L- homocysteine + N(2)-methylguanine(1516) in 16S rRNA. -!- The enzyme specifically methylates guanine(1516) at N(2) in 16S rRNA. Q7UB34 Q7UB34 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. Q7UBD3 Q7UBD3 2.1.1.176 16S rRNA (cytosine(967)-C(5))-methyltransferase. S-adenosyl-L-methionine + cytosine(967) in 16S rRNA = S-adenosyl-L- homocysteine + 5-methylcytosine(967) in 16S rRNA. -!- The enzyme specifically methylates cytosine(967) at C(5) in 16S rRNA. Q7UBI7 Q7UBI7 2.7.7.42 [Glutamine synthetase] adenylyltransferase. [Glutamate--ammonia-ligase] adenylyltransferase. Glutamate-ammonia-ligase adenylyltransferase. Glutamine-synthetase adenylyltransferase. ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine. -!- This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89). -!- The two activities are present on separate domains. Q7UBI7 Q7UBI7 2.7.7.89 [Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase. [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP. -!- This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42). -!- The two activities are present on separate domains. -!- Formerly EC 3.1.4.15. Q7UBI8 Q7UBI8 2.7.1.167 D-glycero-beta-D-manno-heptose-7-phosphate kinase. D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase. D-beta-D-heptose 7-phosphotransferase. D-beta-D-heptose-7-phosphate kinase. Glycero-manno-heptose 7-phosphate kinase. Heptose 7-phosphate kinase. HldE1 heptokinase. D-glycero-beta-D-manno-heptose 7-phosphate + ATP = D-glycero-beta-D- manno-heptose 1,7-bisphosphate + ADP. -!- The bifunctional protein hldE includes D-glycero-beta-D-manno- heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70). -!- The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno- heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. -!- The enzyme selectively produces D-glycero-beta-D-manno-heptose 1,7- bisphosphate. Q7UBI8 Q7UBI8 2.7.7.70 D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase. D-glycero-D-manno-heptose-1-beta-phosphate adenylyltransferase. D-glycero-beta-D-manno-heptose 1-phosphate + ATP = ADP-D-glycero-beta-D- manno-heptose + diphosphate. -!- The bifunctional protein hldE includes D-glycero-beta-D-manno- heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.1.167). -!- The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno- heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. Q7UBT0 Q7UBT0 1.8.4.8 Phosphoadenylyl-sulfate reductase (thioredoxin). 3'-phosphoadenylylsulfate reductase. PAdoPS reductase. PAPS reductase. PAPS reductase, thioredoxin-dependent. PAPS sulfotransferase. Phosphoadenosine-phosphosulfate reductase. Thioredoxin:3'-phospho-adenylylsulfate reductase. Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase. Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. -!- Specific for PAPS. -!- The enzyme from Escherichia coli will use thioredoxins from other species. -!- Formerly EC 1.8.99.4. Q7UBU3 Q7UBU3 6.1.1.7 Alanine--tRNA ligase. Alanine translase. Alanyl-tRNA synthetase. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). Q7UDL2 Q7UDL2 2.7.2.11 Glutamate 5-kinase. Gamma-glutamyl kinase. ATP + L-glutamate = ADP + L-glutamate 5-phosphate. -!- The product rapidly cyclizes to 5-oxoproline and phosphate. Q821A6 Q821A6 2.7.7.72 CCA tRNA nucleotidyltransferase. CCA-adding enzyme. Ribonucleic cytidylic cytidylic adenylic pyrophosphorylase. Transfer ribonucleic adenylyl (cytidylyl) transferase. Transfer RNA adenylyltransferase. Transfer-RNA nucleotidyltransferase. tRNA adenylyl(cytidylyl)transferase. tRNA CCA-diphosphorylase. tRNA cytidylyltransferase. tRNA-nucleotidyltransferase. A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. -!- The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. -!- The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. -!- Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition. -!- Formerly EC 2.7.7.21 and EC 2.7.7.25. Q821C1 Q821C1 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. Q821C2 Q821C2 4.2.1.33 3-isopropylmalate dehydratase. (2R,3S)-3-isopropylmalate hydro-lyase. 3-isopropylmalate hydro-lyase. Alpha-IPM isomerase. Isopropylmalate isomerase. (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. Iron-sulfur. -!- Forms part of the leucine-biosynthesis pathway. -!- Brings about the interconversion of the two isomers of isopropylmalate. Q83IM5 Q83IM5 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q83IP6 Q83IP6 4.1.3.40 Chorismate lyase. CL. CPL. Chorismate = 4-hydroxybenzoate + pyruvate. -!- Catalyzes the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria. -!- The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine. Q83IR6 Q83IR6 5.4.99.21 23S rRNA pseudouridine(2604) synthase. 23S rRNA uridine(2604) = 23S rRNA pseudouridine(2604). -!- The enzyme is not completely specific for uridine(2604) and can, to a small extent, also react with uridine(2605). Q83IS3 Q83IS3 3.6.1.22 NAD(+) diphosphatase. NADH pyrophosphatase. NADP pyrophosphatase. Nicotinamide adenine dinucleotide pyrophosphatase. NAD(H) + H(2)O = AMP + NMN(H). -!- This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences. -!- Also acts on other dinucleotides, including NADP(H), FAD(H(2)), and the thionicotinamide analogs of NAD(+) and NADP(+). Q83IT3 Q83IT3 1.11.1.21 Catalase peroxidase. (1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O. -!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. Q83IY3 Q83IY3 2.3.1.157 Glucosamine-1-phosphate N-acetyltransferase. Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate. -!- The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23. Q83IY3 Q83IY3 2.7.7.23 UDP-N-acetylglucosamine diphosphorylase. N-acetylglucosamine-1-phosphate uridyltransferase. UDP-N-acetylglucosamine pyrophosphorylase. UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine. -!- Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. -!- The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. -!- The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate. Q83J15 Q83J15 2.4.2.10 Orotate phosphoribosyltransferase. OPRT. Orotidine-5'-phosphate diphosphorylase. Orotidine-5'-phosphate pyrophosphorylase. Orotidylic acid phosphorylase. Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. -!- The enzyme from higher eukaryotes also catalyzes the reaction listed as EC 4.1.1.23. Q83J38 Q83J38 6.1.1.14 Glycine--tRNA ligase. Glycyl translase. Glycyl-tRNA synthetase. ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). Q83J89 Q83J89 3.2.1.196 Limit dextrin alpha-1,6-maltotetraose-hydrolase. Glycogen debranching enzyme. Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin. -!- This bacterial enzyme catalyzes a reaction similar to EC 3.2.1.33. -!- However, while EC 3.2.1.33 removes single glucose residues linked by 1,6-alpha-linkage, and thus requires the additional activity of EC 2.4.1.25 to act on limit dextrins formed by EC 2.4.1.1, this enzyme removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin without a need for another enzyme. Q83JA5 Q83JA5 6.1.1.2 Tryptophan--tRNA ligase. L-tryptophan-tRNA(Trp) ligase (AMP-forming). TrpRS. Tryptophan translase. Tryptophanyl ribonucleic synthetase. Tryptophanyl-transfer ribonucleate synthetase. Tryptophanyl-transfer ribonucleic acid synthetase. Tryptophanyl-transfer ribonucleic synthetase. Tryptophanyl-transfer RNA synthetase. Tryptophanyl-tRNA synthase. Tryptophanyl-tRNA synthetase. ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl- tRNA(Trp). Q83JB3 Q83JB3 1.3.1.76 Precorrin-2 dehydrogenase. Precorrin-2 oxidase. Precorrin-2 + NAD(+) = sirohydrochlorin + NADH. -!- Catalyzes the second of three steps leading to the formation of siroheme from uroporphyrinogen III. -!- The first step involves the donation of two S-adenosyl-L-methionine- derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4). -!- In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. -!- In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction. Q83JB3 Q83JB3 2.1.1.107 Uroporphyrinogen-III C-methyltransferase. Adenosylmethionine-uroporphyrinogen III methyltransferase. S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase. SUMT. Urogen III methylase. Uroporphyrin-III C-methyltransferase. Uroporphyrinogen III methylase. Uroporphyrinogen methyltransferase. Uroporphyrinogen-III methylase. Uroporphyrinogen-III methyltransferase. 2 S-adenosyl-L-methionine + uroporphyrinogen III = 2 S-adenosyl-L- homocysteine + precorrin-2. -!- This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. -!- It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. -!- The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4). -!- In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. -!- In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction. -!- Also involved in the biosynthesis of cobalamin. Q83JB3 Q83JB3 4.99.1.4 Sirohydrochlorin ferrochelatase. Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). -!- This enzyme catalyzes the third of three steps leading to the formation of siroheme from uroporphyrinogen III. -!- The first step involves the donation of two S-adenosyl-L-methionine- derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76). -!- In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. -!- In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction. Q83JW6 Q83JW6 2.1.1.186 23S rRNA (cytidine(2498)-2'-O)-methyltransferase. S-adenosyl-L-methionine + cytidine(2498) in 23S rRNA = S-adenosyl-L- homocysteine + 2'-O-methylcytidine(2498) in 23S rRNA. Q83JY2 Q83JY2 3.1.3.5 5'-nucleotidase. A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate. -!- Wide specificity for 5'-nucleotides. Q83JY2 Q83JY2 3.1.3.6 3'-nucleotidase. A 3'-ribonucleotide + H(2)O = a ribonucleoside + phosphate. -!- Wide specificity for 3'-nucleotides. Q83JY2 Q83JY2 3.6.1.11 Exopolyphosphatase. Exopolypase. Metaphosphatase. (Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate. Q83K44 Q83K44 6.1.1.21 Histidine--tRNA ligase. Histidine translase. Histidyl-tRNA synthetase. ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). Q83K86 Q83K86 2.7.1.2 Glucokinase. Glucose kinase. ATP + D-glucose = ADP + D-glucose 6-phosphate. -!- A group of enzymes found in invertebrates and microorganisms highly specific for glucose. Q83K95 Q83K95 2.3.1.16 Acetyl-CoA C-acyltransferase. 3-ketoacyl-CoA thiolase. Beta-ketothiolase. Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. -!- The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. -!- The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl- CoA shortened by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. -!- In the second step the acyl group is transferred to CoA. -!- Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. -!- cf. EC 2.3.1.9. Q83KQ3 Q83KQ3 6.1.1.19 Arginine--tRNA ligase. Arginine translase. Arginyl-tRNA synthetase. ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). Q83KX8 Q83KX8 2.7.1.170 Anhydro-N-acetylmuramic acid kinase. AnhMurNAc kinase. ATP + 1,6-anhydro-N-acetyl-beta-muramate + H(2)O = ADP + N-acetylmuramate 6-phosphate. -!- This enzyme, along with EC 4.2.1.126, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. -!- The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling. -!- The product N-acetylmuramate 6-phosphate is produced as a 7:1 mixture of the alpha- and beta-anomers. -!- Formerly EC 2.7.1.n1. Q83L36 Q83L36 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). Q83L37 Q83L37 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). Q83LF6 Q83LF6 5.4.99.20 23S rRNA pseudouridine(2457) synthase. 23S rRNA uridine(2457) = 23S rRNA pseudouridine(2457). -!- The enzyme modifies uridine(2457) in a stem of 23S RNA in Escherichia coli. Q83LF7 Q83LF7 2.8.1.13 tRNA-uridine 2-sulfurtransferase. A [protein]-S-sulfanyl-L-cysteine + uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + acceptor. -!- The enzyme, found in bacteria, catalyzes formation of the 2-thiouridine modification in the wobble position of tRNA(Gln), tRNA(Lys) and tRNA(Glu). Q83LN3 Q83LN3 6.3.4.21 Nicotinate phosphoribosyltransferase. Niacin ribonucleotidase. Nicotinic acid mononucleotide glycohydrolase. Nicotinic acid mononucleotide pyrophosphorylase. Nicotinic acid phosphoribosyltransferase. Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H(2)O = beta- nicotinate D-ribonucleotide + diphosphate + ADP + phosphate. -!- The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. -!- However, when ATP is available the enzyme is phosphorylated resulting in a much lower K(m) for nicotinate. -!- The phospho-enzyme is hydrolyzed during the transferase reaction, regenerating the low affinity form. -!- The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100. -!- Formerly EC 2.4.2.11. Q83LX5 Q83LX5 6.1.1.4 Leucine--tRNA ligase. Leucine translase. Leucyl-tRNA synthetase. ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). Q83LY3 Q83LY3 2.8.4.3 tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase. 2-methylthio-N-6-isopentenyl adenosine synthase. tRNA-i6A37 methylthiotransferase. N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio- N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor. Iron-sulfur. -!- This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur. -!- The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes. -!- The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. -!- The identity of the electron donor is not known. Q83M42 Q83M42 2.4.2.7 Adenine phosphoribosyltransferase. AMP diphosphorylase. AMP pyrophosphorylase. APRT. Transphosphoribosidase. AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. -!- 5-amino-4-imidazolecarboxamide can replace adenine. Q83ME5 Q83ME5 2.1.2.11 3-methyl-2-oxobutanoate hydroxymethyltransferase. Alpha-ketoisovalerate hydroxymethyltransferase. Dehydropantoate hydroxymethyltransferase. Ketopantoate hydroxymethyltransferase. 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate. Q83MH2 Q83MH2 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q83MJ8 Q83MJ8 5.4.99.25 tRNA pseudouridine(55) synthase. Psi(55) synthase. Psi(55) tRNA pseudouridine synthase. tRNA pseudouridine 55 synthase. tRNA Psi(55) synthase. tRNA uridine(55) = tRNA pseudouridine(55). -!- Pseudourine synthase TruB from Escherichia coli specifically modifies uridine(55) in tRNA molecules. -!- The bifunctional archaeal enzyme also catalyzes the pseudouridylation of uridine(54). -!- It is not known whether the enzyme from Escherichia coli can also act on position 54 in vitro, since this position is occupied in E.coli tRNAs by thymine. Q83MN1 Q83MN1 3.1.26.4 Ribonuclease H. Endoribonuclease H. RNase H. Endonucleolytic cleavage to 5'-phosphomonoester. -!- Acts on RNA-DNA hybrids. Q83PG1 Q83PG1 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase. Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase. (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. -!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211). Q83PG1 Q83PG1 4.2.1.17 Enoyl-CoA hydratase. Enoyl hydrase. Unsaturated acyl-CoA hydratase. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. -!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). Q83PG1 Q83PG1 5.1.2.3 3-hydroxybutyryl-CoA epimerase. (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. Q83PG1 Q83PG1 5.3.3.8 Delta(3)-Delta(2)-enoyl-CoA isomerase. 3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase. (1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. -!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters. Q83PG4 Q83PG4 4.1.1.98 4-hydroxy-3-polyprenylbenzoate decarboxylase. 3-octaprenyl-4-hydroxybenzoate decarboxylase. 4-hydroxy-3-solanesylbenzoate decarboxylase. A 4-hydroxy-3-polyprenylbenzoate = a 2-polyprenylphenol + CO(2). -!- The enzyme catalyzes a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria. -!- The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism. -!- It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129. Q83PJ7 Q83PJ7 2.1.1.170 16S rRNA (guanine(527)-N(7))-methyltransferase. S-adenosyl-L-methionine + guanine(527) in 16S rRNA = S-adenosyl-L- homocysteine + N(7)-methylguanine(527) in 16S rRNA. -!- The enzyme specifically methylates guanine(527) at N(7) in 16S rRNA. Q83PP2 Q83PP2 5.1.3.20 ADP-glyceromanno-heptose 6-epimerase. ADP-L-glycero-D-manno-heptose 6-epimerase. ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose. NAD(+). Q83PR3 Q83PR3 1.1.1.79 Glyoxylate reductase (NADP(+)). Glycolate + NADP(+) = glyoxylate + NADPH. -!- Also reduces hydroxypyruvate to glycerate. -!- Has some affinity for NAD(+). Q83PR3 Q83PR3 1.1.1.81 Hydroxypyruvate reductase. D-glycerate dehydrogenase. D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H. Q83PV3 Q83PV3 2.4.1.18 1,4-alpha-glucan branching enzyme. Amylo-(1,4 to 1,6)transglucosidase. Amylo-(1,4->1,6)-transglycosylase. Branching enzyme. Glycogen branching enzyme. Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. -!- Converts amylose into amylopectin. -!- The description (official name) requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. -!- The latter has frequently been termed Q-enzyme. Q83QA2 Q83QA2 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. Q83QD5 Q83QD5 2.1.1.190 23S rRNA (uracil(1939)-C(5))-methyltransferase. RNA uridine methyltransferase A. S-adenosyl-L-methionine + uracil(1939) in 23S rRNA = S-adenosyl-L- homocysteine + 5-methyluracil(1939) in 23S rRNA. -!- The enzyme specifically methylates uracil(1939) at C(5) in 23S rRNA. -!- The enzyme contains an [4Fe-4S] cluster coordinated by four conserved cysteine residues. Q83QD9 Q83QD9 1.8.1.2 Assimilatory sulfite reductase (NADPH). Sulfite reductase (NADPH). H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. FAD; FMN; Iron-sulfur; Siroheme. -!- The enzyme, which catalyzes the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. -!- Different from EC 1.8.99.5, which is involved in prokaryotic sulfur- based energy metabolism. -!- Formerly EC 1.8.99.1. Q83QE0 Q83QE0 1.8.1.2 Assimilatory sulfite reductase (NADPH). Sulfite reductase (NADPH). H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. FAD; FMN; Iron-sulfur; Siroheme. -!- The enzyme, which catalyzes the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. -!- Different from EC 1.8.99.5, which is involved in prokaryotic sulfur- based energy metabolism. -!- Formerly EC 1.8.99.1. Q83QL1 Q83QL1 6.3.5.2 GMP synthase (glutamine-hydrolyzing). GMP synthetase (glutamine-hydrolyzing). ATP + XMP + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate. -!- Involved in the de novo biosynthesis of guanosine nucleotides. -!- An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. -!- The enzyme can catalyze the second reaction alone in the presence of ammonia. -!- Formerly EC 6.3.4.1. Q83QN4 Q83QN4 4.2.1.126 N-acetylmuramic acid 6-phosphate etherase. MurNAc-6-P etherase. (R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H(2)O. -!- This enzyme, along with EC 2.7.1.170, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. -!- The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling. -!- Formerly EC 4.2.1.n1. Q83QQ5 Q83QQ5 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. Q83QQ8 Q83QQ8 2.1.1.61 tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase. S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2- thiouridylate. -!- Specific for the terminal methyl group of 5-methylaminomethyl-2- thiouridylate. Q83QR1 Q83QR1 1.1.1.290 4-phosphoerythronate dehydrogenase. 4-O-phosphoerythronate dehydrogenase. 4PE dehydrogenase. Erythronate-4-phosphate dehydrogenase. 4-phospho-D-erythronate + NAD(+) = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + NADH. NAD(+). -!- This enzyme catalyzes a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. -!- The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD(+). -!- In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyzes the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)- hydroxy acid. -!- Cf. EC 1.1.1.399. Q83QR3 Q83QR3 5.4.99.12 tRNA pseudouridine(38-40) synthase. PSUI. tRNA pseudouridylate synthase I. tRNA uridine(38-40) = tRNA pseudouridine(38-40). -!- The uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine. -!- TruA specifically modifies uridines at positions 38, 39, and/or 40 in the anticodon stem loop of tRNAs with highly divergent sequences and structures. Q83QT8 Q83QT8 1.1.1.305 UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating). ArnADH. UDP-GlcUA decarboxylase. UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-threo-pentapyranos-4-ulose + CO(2) + NADH. -!- The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13. -!- Formerly EC 1.1.1.n1. Q83QT8 Q83QT8 2.1.2.13 UDP-4-amino-4-deoxy-L-arabinose formyltransferase. ArnAFT. UDP-L-Ara4N formyltransferase. 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinose. -!- The activity is part of a bifunctional enzyme also performing the reaction of EC 1.1.1.305. -!- Formerly EC 2.1.2.n1. Q83QV0 Q83QV0 1.9.6.1 Nitrate reductase (cytochrome). 2 ferrocytochrome + nitrate + 2 H(+) = 2 ferricytochrome + nitrite. Q83QZ5 Q83QZ5 3.5.4.13 dCTP deaminase. Deoxycytidine triphosphate deaminase. dCTP + H(2)O = dUTP + NH(3). Q83R04 Q83R04 5.3.1.16 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase. N-(5'-phospho-D-ribosylformimino)-5-amino-1-(5''-phosphoribosyl)-4- imidazolecarboxamide isomerase. Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase. 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1- deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide. -!- Involved in histidine biosynthesis. Q83R90 Q83R90 1.2.1.19 Aminobutyraldehyde dehydrogenase. 1-pyrroline dehydrogenase. 4-aminobutanal dehydrogenase. ABALDH. Gamma-guanidinobutyraldehyde dehydrogenase. 4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH. -!- The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates. -!- The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54). -!- As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. -!- Formerly EC 1.5.1.35. Q83RC0 Q83RC0 3.5.4.4 Adenosine deaminase. Adenosine aminohydrolase. Adenosine + H(2)O = inosine + NH(3). Q83RE8 Q83RE8 1.1.1.298 3-hydroxypropionate dehydrogenase (NADP(+)). 3-hydroxypropanoate dehydrogenase (NADP(+)). 3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + NADPH. -!- Catalyzes the reduction of 3-oxopropanoate to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles, autotrophic CO(2) fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively. -!- The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyzes the upstream reaction in the pathway, EC 1.2.1.75. -!- Different from EC 1.1.1.59 by cofactor preference. Q83RE8 Q83RE8 1.1.1.381 3-hydroxy acid dehydrogenase. L-allo-threonine + NADP(+) = aminoacetone + CO(2) + NADPH. -!- The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. -!- The highest activity is seen with L-allo-threonine and D-threonine. -!- The enzyme from E.coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2- methylpropanoate. -!- The enzyme has no activity with NAD(+) or L-threonine (cf. EC 1.1.1.103). Q83RJ4 Q83RJ4 2.3.2.27 RING-type E3 ubiquitin transferase. RING E3 ligase. Ubiquitin transferase RING E3. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine. -!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31. Q83RN5 Q83RN5 1.7.5.1 Nitrate reductase (quinone). Dissimilatory nitrate reductase. Nitrate reductase A. Nitrate reductase Z. Quinol-nitrate oxidoreductase. Quinol/nitrate oxidoreductase. Nitrate + a quinol = nitrite + a quinone + H(2)O. Heme; Iron-sulfur; Molybdopterin guanine dinucleotide. -!- A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits. Q83RP1 Q83RP1 1.2.1.70 Glutamyl-tRNA reductase. L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. -!- Forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway, which is used in most eubacteria, and in all archaebacteria, algae and plants. -!- However, in the alpha-proteobacteria EC 2.3.1.37 is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. -!- This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. -!- Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. Q83RX5 Q83RX5 2.1.1.173 23S rRNA (guanine(2445)-N(2))-methyltransferase. S-adenosyl-L-methionine + guanine(2445) in 23S rRNA = S-adenosyl-L- homocysteine + N(2)-methylguanine(2445) in 23S rRNA. -!- The enzyme methylates 23S rRNA in vitro, assembled 50S subunits are not a substrate. -!- The enzyme specifically methylates guanine(2445) at N(2) in 23S rRNA. -!- Formerly EC 2.1.1.52. Q83RX5 Q83RX5 2.1.1.264 23S rRNA (guanine(2069)-N(7))-methyltransferase. 23S rRNA m(7)G(2069) methyltransferase. S-adenosyl-L-methionine + guanine(2069) in 23S rRNA = S-adenosyl-L- homocysteine + N(7)-methylguanine(2069) in 23S rRNA. -!- The enzyme specifically methylates guanine(2069) at position N7 in 23S rRNA. -!- In gamma-proteobacteria the enzyme also catalyzes EC 2.1.1.173, while in beta-proteobacteria the activities are carried out by separate proteins. -!- The enzyme from the gamma-proteobacterium Escherichia coli has RNA unwinding activity as well. Q83RX6 Q83RX6 1.3.5.2 Dihydroorotate dehydrogenase (quinone). DHOD. DHOdehase. DHODH. (S)-dihydroorotate + a quinone = orotate + a quinol. FMN. -!- This Class 2 dihydroorotate dehydrogenase enzyme contains FMN. -!- The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane. -!- The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. -!- The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates. -!- Methyl-, ethyl-, tert-butyl and benzyl-(S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not. -!- Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor. -!- Formerly EC 1.3.99.11. Q83SE1 Q83SE1 3.5.1.2 Glutaminase. L-glutamine amidohydrolase. L-glutamine + H(2)O = L-glutamate + NH(3). Q83SE5 Q83SE5 4.99.1.1 Protoporphyrin ferrochelatase. Ferrochelatase. Heme synthase. Iron chelatase. Protoheme ferro-lyase. Protoheme + 2 H(+) = protoporphyrin + Fe(2+). -!- The enzyme catalyzes the terminal step in the heme biosynthesis pathways of eukaryotes and Gram-negative bacteria. Q83SG2 Q83SG2 2.2.1.7 1-deoxy-D-xylulose-5-phosphate synthase. 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating). 1-deoxyxylulose-5-phosphate synthase. DXP-synthase. Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO(2). Thiamine diphosphate. -!- The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. -!- Formerly EC 4.1.3.37. Q83SM9 Q83SM9 1.7.1.7 GMP reductase. Guanosine 5'-monophosphate oxidoreductase. Guanosine 5'-monophosphate reductase. Guanosine 5'-phosphate reductase. Guanosine monophosphate reductase. Guanylate reductase. NADPH:GMP oxidoreductase (deaminating). NADPH:guanosine-5'-phosphate oxidoreductase (deaminating). Inosine 5'-phosphate + NH(3) + NADP(+) = guanosine 5'-phosphate + NADPH. -!- Formerly EC 1.6.6.8. Q83SN7 Q83SN7 2.1.1.199 16S rRNA (cytosine(1402)-N(4))-methyltransferase. S-adenosyl-L-methionine + cytosine(1402) in 16S rRNA = S-adenosyl-L- homocysteine + N(4)-methylcytosine(1402) in 16S rRNA. -!- RsmH catalyzes the N(4)-methylation of cytosine(1402) and RsmI (EC 2.1.1.198) catalyzes the 2'-O-methylation of cytosine(1402) in 16S rRNA. -!- Both methylations are necessary for efficient translation initiation at the UUG and GUG codons. Q83SP1 Q83SP1 1.1.1.85 3-isopropylmalate dehydrogenase. Beta-IPM dehydrogenase. Beta-isopropylmalate dehydrogenase. IMDH. (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH. Q8CXS7 Q8CXS7 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. Q8EIX3 Q8EIX3 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. Q8F663 Q8F663 3.4.21.88 Repressor LexA. Hydrolysis of Ala-|-Gly bond in repressor LexA. -!- In the presence of single-stranded DNA, the RecA protein interacts with LexA causing an autocatalytic cleavage which disrupts the DNA- binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. -!- The activity was previously attributed to the RecA protein (formerly EC 3.4.99.37). -!- Belongs to peptidase family S24. Q8GP19 Q8GP19 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. Q8NU97 Q8NU97 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. Q8NU98 Q8NU98 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. Q8PES0 Q8PES0 2.3.1.15 Glycerol-3-phosphate 1-O-acyltransferase. Glycerol-3-phosphate O-acyltransferase. Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. -!- Acyl-[acyl-carrier-protein] can also act as acyl donor. -!- Acts only with derivatives of fatty acids of chain length above C(10). Q8PGJ4 Q8PGJ4 2.7.7.7 DNA-directed DNA polymerase. DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49. Q8PH13 Q8PH13 4.1.99.17 Phosphomethylpyrimidine synthase. 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO. Iron-sulfur. -!- Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. -!- The first stage of catalysis is reduction of the S-adenosyl-L- methionine to produce L-methionine and a 5'-deoxyadenosin-5'-yl radical that is crucial for the conversion of the substrate. -!- Part of the pathway for thiamine biosynthesis. Q8PNI0 Q8PNI0 3.1.2.6 Hydroxyacylglutathione hydrolase. Glyoxalase II. S-(2-hydroxyacyl)glutathione + H(2)O = glutathione + a 2-hydroxy carboxylate. -!- Also hydrolyzes S-acetoacetylglutathione, more slowly. -!- Formerly EC 3.1.2.8. Q8PNS9 Q8PNS9 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q8PP38 Q8PP38 1.14.14.5 Alkanesulfonate monooxygenase. FMNH(2)-dependent aliphatic sulfonate monooxygenase. Sulfate starvation-induced protein 6. An alkanesulfonate (R-CH(2)-SO(3)H) + FMNH(2) + O(2) = an aldehyde (R-CHO) + FMN + sulfite + H(2)O. -!- The enzyme from Escherichia coli catalyzes the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C(1)- to C(14)- sulfonates as well as substituted C(2)-sulfonates). -!- Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. -!- Does not use FMN as a bound cofactor. -!- Instead, it uses reduced FMN (i.e., FMNH(2)) as a substrate. -!- FMNH(2) is provided by SsuE, the associated FMN reductase (EC 1.5.1.38). Q8PP84 Q8PP84 3.3.1.1 Adenosylhomocysteinase. Adenosylhomocysteine hydrolase. AdoHcyase. S-adenosylhomocysteinase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine synthase. SAHase. S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine. NAD(+). -!- The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4. Q8PPR3 Q8PPR3 2.5.1.61 Hydroxymethylbilane synthase. (4-(2-carboxyethyl)-3-(carboxymethyl)pyrrol-2-yl)methyltransferase (hydrolyzing). HMB-synthase. Porphobilinogen deaminase. Pre-uroporphyrinogen synthase. Uroporphyrinogen I synthase. Uroporphyrinogen I synthetase. Uroporphyrinogen synthase. Uroporphyrinogen synthetase. 4 porphobilinogen + H(2)O = hydroxymethylbilane + 4 NH(3). Dipyrromethane. -!- The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active center. -!- The terminal tetrapyrrole is then hydrolyzed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. -!- In the presence of a second enzyme, EC 4.2.1.75, which is often called cosynthase, the product is cyclized to form uroporphyrinogen III. -!- If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I. -!- Formerly EC 4.3.1.8. Q8PUQ8 Q8PUQ8 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q8PVK0 Q8PVK0 6.1.1.1 Tyrosine--tRNA ligase. L-tyrosine-tRNA(Tyr) ligase (AMP-forming). Tyrosine translase. Tyrosine tRNA synthetase. Tyrosine-transfer ribonucleate synthetase. Tyrosine-transfer RNA ligase. Tyrosyl-transfer ribonucleate synthetase. Tyrosyl-transfer ribonucleic acid synthetase. Tyrosyl-transfer RNA synthetase. Tyrosyl-tRNA ligase. Tyrosyl-tRNA synthetase. ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). Q8R967 Q8R967 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. Q8R9S4 Q8R9S4 5.1.1.7 Diaminopimelate epimerase. LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. Q8RAC9 Q8RAC9 3.1.11.6 Exodeoxyribonuclease VII. E.coli exonuclease VII. Exonuclease VII. Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates. -!- Preference for single-stranded DNA. -!- Similar enzyme: Micrococcus luteus exonuclease. Q8VSC3 Q8VSC3 2.3.2.27 RING-type E3 ubiquitin transferase. RING E3 ligase. Ubiquitin transferase RING E3. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine. -!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31. Q8X3W8 Q8X3W8 6.1.1.7 Alanine--tRNA ligase. Alanine translase. Alanyl-tRNA synthetase. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). Q8X4P8 Q8X4P8 4.2.1.2 Fumarate hydratase. Fumarase. (S)-malate = fumarate + H(2)O. Q8X4P8 Q8X4P8 5.3.2.2 Oxaloacetate tautomerase. Oxalacetic keto--enol isomerase. Oxaloacetate keto--enol tautomerase. Keto-oxaloacetate = enol-oxaloacetate. Q8X4V5 Q8X4V5 5.4.3.8 Glutamate-1-semialdehyde 2,1-aminomutase. Glutamate-1-semialdehyde aminotransferase. (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Pyridoxal 5'-phosphate. Q8X505 Q8X505 1.1.1.298 3-hydroxypropionate dehydrogenase (NADP(+)). 3-hydroxypropanoate dehydrogenase (NADP(+)). 3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + NADPH. -!- Catalyzes the reduction of 3-oxopropanoate to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles, autotrophic CO(2) fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively. -!- The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyzes the upstream reaction in the pathway, EC 1.2.1.75. -!- Different from EC 1.1.1.59 by cofactor preference. Q8X505 Q8X505 1.1.1.381 3-hydroxy acid dehydrogenase. L-allo-threonine + NADP(+) = aminoacetone + CO(2) + NADPH. -!- The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. -!- The highest activity is seen with L-allo-threonine and D-threonine. -!- The enzyme from E.coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2- methylpropanoate. -!- The enzyme has no activity with NAD(+) or L-threonine (cf. EC 1.1.1.103). Q8X611 Q8X611 2.1.2.3 Phosphoribosylaminoimidazolecarboxamide formyltransferase. 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4- imidazolecarboxamide formyltransferase. 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase. 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase. 5-amino-4-imidazolecarboxamide ribonucleotide transformylase. 5-amino-4-imidazolecarboxamide ribotide transformylase. AICAR formyltransferase. AICAR transformylase. Aminoimidazolecarboxamide ribonucleotide transformylase. 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide. Q8X611 Q8X611 3.5.4.10 IMP cyclohydrolase. IMP synthetase. Inosinicase. IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. Q8X6M8 Q8X6M8 3.4.24.55 Pitrilysin. Protease III. Protease Pi. Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon. Zn(2+). -!- From the periplasmic space of Escherichia coli. -!- Inhibited by EDTA and 1,10-phenanthroline; not thiol dependent. -!- Belongs to peptidase family M16. -!- Formerly EC 3.4.99.44. Q8X6Z6 Q8X6Z6 3.4.21.105 Rhomboid protease. Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains. -!- These endopeptidases are multi-spanning membrane proteins. -!- Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. -!- Important for embryo development in Drosophila melanogaster. -!- Rhomboid is a key regulator of EGF receptor signaling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. -!- Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. -!- Belongs to peptidase family S54. Q8X733 Q8X733 4.1.1.49 Phosphoenolpyruvate carboxykinase (ATP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2). Q8X743 Q8X743 4.1.1.31 Phosphoenolpyruvate carboxylase. PEP carboxylase. PEPCase. Phosphoenolpyruvic carboxylase. Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-). -!- This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. -!- The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate. Q8X7N4 Q8X7N4 1.2.1.41 Glutamate-5-semialdehyde dehydrogenase. Beta-glutamylphosphate reductase. Gamma-glutamylphosphate reductase. Glutamyl-gamma-semialdehyde dehydrogenase. L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH. Q8X7P7 Q8X7P7 5.1.3.26 N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase. GlcNAc-P-P-Und 4-epimerase. N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = N-acetyl-alpha-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol. -!- The enzyme is involved in biosynthesis of the repeating tetrasaccharide unit of the O-antigen produced by some Gram-negative bacteria. Q8X825 Q8X825 2.8.1.6 Biotin synthase. Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin. Iron-sulfur. -!- The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster. -!- In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and a putative dethiobiotinyl carbon radical. -!- Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring. -!- The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover. -!- In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis. Q8X8W2 Q8X8W2 6.1.1.15 Proline--tRNA ligase. Proline translase. Prolyl-tRNA synthetase. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). Q8X8Y7 Q8X8Y7 2.3.1.117 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. Tetrahydrodipicolinate N-succinyltransferase. Tetrahydrodipicolinate succinylase. Tetrahydrodipicolinate succinyltransferase. Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. -!- Involved in the biosynthesis of lysine in bacteria, cyanobacteria and higher plants. -!- Earlier erroneously called 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase. Q8X902 Q8X902 4.4.1.21 S-ribosylhomocysteine lyase. S-ribosylhomocysteinase. S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5- dihydroxypentan-2,3-dione. Fe(2+). -!- The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density. -!- Formerly EC 3.2.1.148 and EC 3.3.1.3. Q8X984 Q8X984 1.7.1.7 GMP reductase. Guanosine 5'-monophosphate oxidoreductase. Guanosine 5'-monophosphate reductase. Guanosine 5'-phosphate reductase. Guanosine monophosphate reductase. Guanylate reductase. NADPH:GMP oxidoreductase (deaminating). NADPH:guanosine-5'-phosphate oxidoreductase (deaminating). Inosine 5'-phosphate + NH(3) + NADP(+) = guanosine 5'-phosphate + NADPH. -!- Formerly EC 1.6.6.8. Q8XA55 Q8XA55 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. Q8XAC5 Q8XAC5 6.3.3.1 Phosphoribosylformylglycinamidine cyclo-ligase. AIR synthase. AIR synthetase. AIRS. Phosphoribosyl-aminoimidazole synthetase. Phosphoribosylaminoimidazole synthetase. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. Q8XAT4 Q8XAT4 3.6.4.13 RNA helicase. ATP + H(2)O = ADP + phosphate. -!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase). Q8XB34 Q8XB34 4.1.99.1 Tryptophanase. L-tryptophan indole-lyase. TNase. L-tryptophan + H(2)O = indole + pyruvate + NH(3). K(+); Pyridoxal 5'-phosphate. -!- The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- Also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine and other 3-substituted amino acids. Q8XBV3 Q8XBV3 2.7.7.58 (2,3-dihydroxybenzoyl)adenylate synthase. 2,3-dihydroxybenzoate-AMP ligase. ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3- dihydroxybenzoyl)adenylate. Q8XBV3 Q8XBV3 6.3.2.14 Enterobactin synthase. 2,3-dihydroxybenzoate--serine ligase. N-(2,3-dihydroxybenzoyl)-serine synthetase. 6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate. -!- This enzyme complex catalyzes the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. -!- In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyzes the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyzes the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3- dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule). Q8XCF9 Q8XCF9 3.1.1.61 Protein-glutamate methylesterase. CheB methylesterase. Chemotaxis-specific methylesterase. Methyl-accepting chemotaxis protein methyl-esterase. Methylesterase CheB. PME. Protein carboxyl methylesterase. Protein methyl-esterase. Protein methylesterase. Protein L-glutamate O(5)-methyl ester + H(2)O = protein L-glutamate + methanol. -!- Hydrolyzes the products of EC 2.1.1.77, EC 2.1.1.78, EC 2.1.1.80 and EC 2.1.1.100. Q8XCF9 Q8XCF9 3.5.1.44 Protein-glutamine glutaminase. Glutaminylpeptide glutaminase. Peptidoglutaminase II. Protein L-glutamine + H(2)O = protein L-glutamate + NH(3). -!- Specific for the hydrolysis of the gamma-amide of glutamine substituted at the carboxyl position or both the alpha-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L- glutaminylglycine. Q8XD03 Q8XD03 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. Q8XD33 Q8XD33 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. Q8XD88 Q8XD88 2.7.4.8 Guanylate kinase. Deoxyguanylate kinase. GMP kinase. Guanosine monophosphate kinase. ATP + GMP = ADP + GDP. -!- dGMP can also act as acceptor. -!- dATP can act as donor. Q8XDE7 Q8XDE7 2.5.1.55 3-deoxy-8-phosphooctulonate synthase. 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating). 2-dehydro-3-deoxy-phosphooctonate aldolase. 2-keto-3-deoxy-8-phosphooctonic synthetase. 3-deoxy-D-manno-octulosonate-8-phosphate synthase. 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase. 3-deoxy-D-mannooctulosonate-8-phosphate synthetase. 3-deoxyoctulosonic 8-phosphate synthetase. KDO-8-P synthase. KDO-8-phosphate synthetase. KDOP synthase. Phospho-2-keto-3-deoxyoctonate aldolase. Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 3-deoxy-D-manno- octulosonate 8-phosphate + phosphate. -!- Formerly EC 4.1.2.16. Q8XDE9 Q8XDE9 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. Q8XDS0 Q8XDS0 4.3.1.1 Aspartate ammonia-lyase. Aspartase. Fumaric aminase. L-aspartate = fumarate + NH(3). Q8XE27 Q8XE27 6.1.1.3 Threonine--tRNA ligase. Threonine translase. Threonyl-tRNA synthetase. ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). Q8XEA7 Q8XEA7 2.6.1.52 Phosphoserine transaminase. 3-phosphoserine aminotransferase. 3PHP transaminase. Hydroxypyruvic phosphate--glutamic transaminase. L-phosphoserine aminotransferase. Phosphohydroxypyruvate transaminase. Phosphohydroxypyruvic--glutamic transaminase. Phosphoserine aminotransferase. PSAT. (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + L-glutamate. Pyridoxal 5'-phosphate. -!- Catalyzes the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli. -!- Also catalyzes the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in E.coli (using reaction 2 above). -!- In E.coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). -!- Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis. -!- Non-phosphorylated forms of serine and threonine are not substrates. Q8XEG2 Q8XEG2 2.6.1.16 Glutamine--fructose-6-phosphate transaminase (isomerizing). D-fructose-6-phosphate amidotransferase. GlcN6P synthase. Glucosamine-6-phosphate isomerase (glutamine-forming). Glucosamine-6-phosphate synthase. Hexosephosphate aminotransferase. L-glutamine-D-fructose-6-phosphate amidotransferase. L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. -!- Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). -!- Formerly EC 5.3.1.19. Q8Y3P9 Q8Y3P9 1.11.1.6 Catalase. 2 H(2)O(2) = O(2) + 2 H(2)O. Heme; Mn(2+). -!- A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase. -!- The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. -!- Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21. Q8Y3T4 Q8Y3T4 6.1.1.11 Serine--tRNA ligase. Serine translase. SerRS. Seryl-transfer ribonucleate synthetase. Seryl-transfer ribonucleic acid synthetase. Seryl-transfer RNA synthetase. Seryl-tRNA synthetase. (1) ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). (2) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). -!- This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1. Q8Y495 Q8Y495 6.3.4.2 CTP synthase (glutamine hydrolyzing). CTP synthetase. UTP--ammonia ligase. ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. -!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution. Q8Y4B2 Q8Y4B2 2.1.2.1 Glycine hydroxymethyltransferase. Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase. 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Pyridoxal 5'-phosphate. -!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine. Q8Y4B3 Q8Y4B3 2.4.2.9 Uracil phosphoribosyltransferase. UMP diphosphorylase. UMP pyrophosphorylase. UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. Q8Y4C0 Q8Y4C0 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q8Y4C6 Q8Y4C6 4.2.1.59 3-hydroxyacyl-[acyl-carrier-protein] dehydratase. (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase. Beta-hydroxyoctanoyl thioester dehydratase. Beta-hydroxyoctanoyl-ACP-dehydrase. Beta-hydroxyoctanoyl-acyl carrier protein dehydrase. D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase. A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O. -!- This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- The enzyme uses fatty acyl thioesters of ACP in vivo. -!- Different forms of the enzyme may have preferences for substrates with different chain length. -!- For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. -!- Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14. -!- Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0). -!- FabZ, but not FabA, can also accept unsaturated substrates. -!- Formerly EC 4.2.1.58, EC 4.2.1.60 and EC 4.2.1.61. Q8Y4I2 Q8Y4I2 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. Q8Y4I4 Q8Y4I4 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. Q8Y4R7 Q8Y4R7 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. Q8Y5E6 Q8Y5E6 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. Q8Y5M1 Q8Y5M1 6.3.2.9 UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase. D-glutamate ligase. D-glutamate-adding enzyme. MurD synthetase. UDP-Mur-NAC-L-Ala:D-Glu ligase. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase. UDP-N-acetylmuramoylalanine--D-glutamate ligase. Uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase. ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate. -!- Involved in the synthesis of a cell-wall peptide in bacteria. Q8Y5N8 Q8Y5N8 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q8Y5W6 Q8Y5W6 2.7.4.25 (d)CMP kinase. dCMP kinase. Deoxycytidine monophosphokinase. Deoxycytidylate kinase. ATP + (d)CMP = ADP + (d)CDP. -!- The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. -!- Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22. -!- The enzyme phosphorylates dCMP nearly as well as it does CMP. Q8Y5X4 Q8Y5X4 2.7.4.6 Nucleoside-diphosphate kinase. NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. -!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. Q8Y6D0 Q8Y6D0 6.5.1.2 DNA ligase (NAD(+)). DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (NAD(+)). Polydeoxyribonucleotide synthase (NAD+). Polynucleotide ligase (NAD(+)). Polynucleotide ligase (NAD+). NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide. -!- The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7. Q8Y6K9 Q8Y6K9 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase. SEPHCHC synthase. Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl- cyclohex-3-ene-1-carboxylate + CO(2). Mg(2+). -!- Involved in the biosynthesis of vitamin K(2) (menaquinone). -!- In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. -!- It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO(2) but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20. -!- Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC. -!- Formerly EC 2.5.1.64 and EC 2.5.1.n1. Q8Y6S8 Q8Y6S8 6.3.2.8 UDP-N-acetylmuramate--L-alanine ligase. Alanine-adding enzyme. L-Ala ligase. L-alanine-adding enzyme. MurC synthetase. UDP-acetylmuramyl-L-alanine synthetase. UDP-MurNAc:L-alanine ligase. UDP-N-acetylmuramoyl-L-alanine synthetase. UDP-N-acetylmuramoylalanine synthetase. UDP-N-acetylmuramyl:L-alanine ligase. UDPMurNAc-L-alanine synthetase. Uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase. Uridine diphosphate N-acetylmuramate:L-alanine ligase. Uridine diphospho-N-acetylmuramoylalanine synthetase. Uridine-diphosphate-N-acetylmuramate:L-alanine ligase. ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP- N-acetyl-alpha-D-muramoyl-L-alanine. -!- Involved in the synthesis of a cell-wall peptide. Q8Y6V0 Q8Y6V0 2.7.2.1 Acetate kinase. Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK. ATP + acetate = ADP + acetyl phosphate. Mg(2+). -!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. Q8Y6W0 Q8Y6W0 2.7.1.11 6-phosphofructokinase. Phosphofructokinase I. Phosphohexokinase. ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. -!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. -!- UTP, CTP and ITP can act as donors. -!- Not identical with EC 2.7.1.105. Q8Y6X5 Q8Y6X5 2.5.1.61 Hydroxymethylbilane synthase. (4-(2-carboxyethyl)-3-(carboxymethyl)pyrrol-2-yl)methyltransferase (hydrolyzing). HMB-synthase. Porphobilinogen deaminase. Pre-uroporphyrinogen synthase. Uroporphyrinogen I synthase. Uroporphyrinogen I synthetase. Uroporphyrinogen synthase. Uroporphyrinogen synthetase. 4 porphobilinogen + H(2)O = hydroxymethylbilane + 4 NH(3). Dipyrromethane. -!- The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active center. -!- The terminal tetrapyrrole is then hydrolyzed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. -!- In the presence of a second enzyme, EC 4.2.1.75, which is often called cosynthase, the product is cyclized to form uroporphyrinogen III. -!- If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I. -!- Formerly EC 4.3.1.8. Q8Y6X9 Q8Y6X9 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q8Y735 Q8Y735 2.7.7.18 Nicotinate-nucleotide adenylyltransferase. Deamido-NAD(+) diphosphorylase. Deamido-NAD(+) pyrophosphorylase. ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+). Q8Y742 Q8Y742 3.6.5.n1 Elongation factor 4. GTP + H(2)O = GDP + phosphate. -!- The enzyme is required for accurate and efficient protein synthesis under certain stress conditions. -!- May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. -!- Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. -!- Binds to ribosomes in a GTP-dependent manner. Q8Y766 Q8Y766 4.3.3.7 4-hydroxy-tetrahydrodipicolinate synthase. DHDPS. Dihydrodipicolinate synthetase. Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5- tetrahydro-(2S)-dipicolinate + H(2)O. -!- Formerly EC 4.2.1.52. Q8Y7A5 Q8Y7A5 5.3.3.2 Isopentenyl-diphosphate Delta-isomerase. IPP isomerase. Isopentenylpyrophosphate Delta-isomerase. Isopentenylpyrophosphate isomerase. Methylbutenylpyrophosphate isomerase. Isopentenyl diphosphate = dimethylallyl diphosphate. FAD or FMN; Mg(2+) or Ca(2+) or Mn(2+). Q8Y7D3 Q8Y7D3 1.4.4.2 Glycine dehydrogenase (aminomethyl-transferring). Glycine cleavage system P-protein. Glycine decarboxylase. Glycine dehydrogenase (decarboxylating). Glycine-cleavage complex P-protein. Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L- lysine + CO(2). Pyridoxal 5'-phosphate. -!- A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Previously known as glycine synthase. Q8Y7F1 Q8Y7F1 2.7.7.8 Polyribonucleotide nucleotidyltransferase. Polynucleotide phosphorylase. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. -!- ADP, IDP, GDP, UDP and CDP can act as donors. Q8Y7L0 Q8Y7L0 5.2.1.8 Peptidylprolyl isomerase. Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase. Peptidylproline (omega=180) = peptidylproline (omega=0). -!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. Q8Y7N6 Q8Y7N6 2.7.7.56 tRNA nucleotidyltransferase. Phosphate-dependent exonuclease. Ribonuclease PH. RNase PH. tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate. -!- Brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3'-terminus in tRNA and nucleoside diphosphate. -!- Not identical with EC 2.7.7.8. Q8Y7Q2 Q8Y7Q2 6.1.1.20 Phenylalanine--tRNA ligase. Phenylalanine translase. Phenylalanyl-tRNA synthetase. ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe). Q8Y822 Q8Y822 6.3.5.2 GMP synthase (glutamine-hydrolyzing). GMP synthetase (glutamine-hydrolyzing). ATP + XMP + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate. -!- Involved in the de novo biosynthesis of guanosine nucleotides. -!- An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. -!- The enzyme can catalyze the second reaction alone in the presence of ammonia. -!- Formerly EC 6.3.4.1. Q8Y832 Q8Y832 2.7.7.40 D-ribitol-5-phosphate cytidylyltransferase. CDP-ribitol diphosphorylase. CDP-ribitol pyrophosphorylase. CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol. Q8Y8A1 Q8Y8A1 2.3.1.89 Tetrahydrodipicolinate N-acetyltransferase. Tetrahydrodipicolinate acetylase. Acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + L-2-acetamido-6-oxoheptanedioate. Q8Y8E7 Q8Y8E7 3.5.99.6 Glucosamine-6-phosphate deaminase. GlcN6P deaminase. Glucosamine phosphate deaminase. Glucosamine-6-phosphate isomerase. Phosphoglucosamine isomerase. Phosphoglucosaminisomerase. Alpha-D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). -!- Isomerization of the aldose-ketose type converts the -CH(-NH(2))-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH(2)-OH, forming 2-deoxy-2-imino-D-arabino-hexitol which then hydrolyzes to yield fructose 6-phosphate and ammonia. -!- N-acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme. -!- Formerly EC 5.3.1.10. Q8Y8N0 Q8Y8N0 3.6.4.13 RNA helicase. ATP + H(2)O = ADP + phosphate. -!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase). Q8Y915 Q8Y915 2.6.1.16 Glutamine--fructose-6-phosphate transaminase (isomerizing). D-fructose-6-phosphate amidotransferase. GlcN6P synthase. Glucosamine-6-phosphate isomerase (glutamine-forming). Glucosamine-6-phosphate synthase. Hexosephosphate aminotransferase. L-glutamine-D-fructose-6-phosphate amidotransferase. L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. -!- Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). -!- Formerly EC 5.3.1.19. Q8Y9C1 Q8Y9C1 1.7.1.17 FMN-dependent NADH-azoreductase. Anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH. FMN. -!- The enzyme catalyzes the reductive cleavage of an azo bond in aromatic azo compounds to form the corresponding amines. -!- Does not accept NADPH. -!- Cf. EC 1.7.1.6. Q8Y9L8 Q8Y9L8 2.7.6.1 Ribose-phosphate diphosphokinase. Phosphoribosyl diphosphate synthetase. Phosphoribosyl pyrophosphate synthetase. Ribose-phosphate pyrophosphokinase. ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. -!- dATP can also act as donor. Q8YA96 Q8YA96 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q8YAB1 Q8YAB1 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). Q8YAM8 Q8YAM8 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q92LB1 Q92LB1 2.7.7.18 Nicotinate-nucleotide adenylyltransferase. Deamido-NAD(+) diphosphorylase. Deamido-NAD(+) pyrophosphorylase. ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+). Q92M99 Q92M99 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. Q92TB0 Q92TB0 4.2.1.19 Imidazoleglycerol-phosphate dehydratase. D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2- oxopropyl phosphate + H(2)O. Q92TC7 Q92TC7 2.1.3.15 Acetyl-CoA carboxytransferase. [Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl- CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl- CoA. -!- The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. -!- In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2). -!- Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3). Q92TF2 Q92TF2 2.7.4.27 ([Pyruvate, phosphate dikinase] phosphate) phosphotransferase. Bifunctional dikinase regulatory protein. PPDK regulatory protein. Pyruvate, phosphate dikinase regulatory protein. [Pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate. -!- The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyzes the phosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.11.32. -!- Formerly EC 2.7.4.n1. Q92TF2 Q92TF2 2.7.11.32 [Pyruvate, phosphate dikinase] kinase. Bifunctional dikinase regulatory protein. PPDK regulatory protein. Pyruvate, phosphate dikinase regulatory protein. ADP + [pyruvate, phosphate dikinase] = AMP + [pyruvate, phosphate dikinase] phosphate. -!- The enzyme from the plants Zea mays (maize) and Arabidopsis is bifunctional and catalyzes both the phosphorylation and dephosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.4.27. -!- The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates an active site histidine. -!- Formerly EC 2.7.11.n1. Q93FE6 Q93FE6 2.7.4.3 Adenylate kinase. Adenylic kinase. Adenylokinase. Myokinase. ATP + AMP = 2 ADP. -!- Inorganic triphosphate can also act as donor. Q97DB2 Q97DB2 2.1.3.15 Acetyl-CoA carboxytransferase. [Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl- CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl- CoA. -!- The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. -!- In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2). -!- Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3). Q97ED5 Q97ED5 6.1.1.15 Proline--tRNA ligase. Proline translase. Prolyl-tRNA synthetase. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). Q97EG9 Q97EG9 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q97EH0 Q97EH0 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q97EK6 Q97EK6 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q97ES0 Q97ES0 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q97F13 Q97F13 4.4.1.21 S-ribosylhomocysteine lyase. S-ribosylhomocysteinase. S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5- dihydroxypentan-2,3-dione. Fe(2+). -!- The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density. -!- Formerly EC 3.2.1.148 and EC 3.3.1.3. Q97F85 Q97F85 2.5.1.6 Methionine adenosyltransferase. AdoMet synthetase. S-adenosylmethionine synthetase. ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine. -!- Formerly EC 2.4.2.13. Q97FP8 Q97FP8 5.3.1.9 Glucose-6-phosphate isomerase. Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase. D-glucose 6-phosphate = D-fructose 6-phosphate. -!- Also catalyzes the anomerization of D-glucose 6-phosphate. Q97IG3 Q97IG3 6.1.1.7 Alanine--tRNA ligase. Alanine translase. Alanyl-tRNA synthetase. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). Q97IR8 Q97IR8 3.1.3.11 Fructose-bisphosphatase. Fructose 1,6-bisphosphatase. Hexose diphosphatase. D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. -!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. Q97J91 Q97J91 2.1.2.3 Phosphoribosylaminoimidazolecarboxamide formyltransferase. 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4- imidazolecarboxamide formyltransferase. 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase. 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase. 5-amino-4-imidazolecarboxamide ribonucleotide transformylase. 5-amino-4-imidazolecarboxamide ribotide transformylase. AICAR formyltransferase. AICAR transformylase. Aminoimidazolecarboxamide ribonucleotide transformylase. 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide. Q97J91 Q97J91 3.5.4.10 IMP cyclohydrolase. IMP synthetase. Inosinicase. IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. Q97L52 Q97L52 4.2.1.11 Phosphopyruvate hydratase. 2-phosphoglycerate dehydratase. Enolase. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Mg(2+). -!- Also acts on 3-phospho-D-erythronate. Q97U21 Q97U21 1.1.1.47 Glucose 1-dehydrogenase (NAD(P)(+)). D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H. -!- This enzyme has similar activity with either NAD(+) or NADP(+). -!- Cf. EC 1.1.1.118 and EC 1.1.1.119. Q97U29 Q97U29 2.7.1.178 2-dehydro-3-deoxyglucono/galactono-kinase. 2-keto-3-deoxy-D-gluconate kinase. KDG kinase. (1) ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6- phospho-D-gluconate. (2) ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6- phospho-D-galactonate. -!- The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. -!- It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3- deoxy-D-galactonate with similar catalytic efficiency. -!- Cf. EC 2.7.1.45 and EC 2.7.1.58. Q97U96 Q97U96 4.2.1.5 Arabinonate dehydratase. D-arabinonate hydro-lyase. D-arabinonate = 2-dehydro-3-deoxy-D-arabinonate + H(2)O. Q97UA1 Q97UA1 1.2.1.26 2,5-dioxovalerate dehydrogenase. 2,5-dioxopentanoate + NADP(+) + H(2)O = 2-oxoglutarate + NADPH. Q97UA2 Q97UA2 3.4.11.5 Prolyl aminopeptidase. Cytosol aminopeptidase V. Pro-X aminopeptidase. Proline aminopeptidase. Proline iminopeptidase. Release of N-terminal proline from a peptide. Mn(2+). -!- Present in the cytosol of mammalian and microbial cells. -!- In contrast to the mammalian form, the bacterial form of the enzyme hydrolyzes both polyproline and prolyl-2-naphthylamide. -!- The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1. -!- Belongs to peptidase family S33. -!- Formerly EC 3.4.1.4. Q97UB2 Q97UB2 4.2.1.9 Dihydroxy-acid dehydratase. 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H(2)O. Q97VS5 Q97VS5 4.1.1.32 Phosphoenolpyruvate carboxykinase (GTP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2). -!- ITP can act as phosphate donor. Q97VW8 Q97VW8 6.1.1.3 Threonine--tRNA ligase. Threonine translase. Threonyl-tRNA synthetase. ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). Q97VY2 Q97VY2 4.2.1.33 3-isopropylmalate dehydratase. (2R,3S)-3-isopropylmalate hydro-lyase. 3-isopropylmalate hydro-lyase. Alpha-IPM isomerase. Isopropylmalate isomerase. (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. Iron-sulfur. -!- Forms part of the leucine-biosynthesis pathway. -!- Brings about the interconversion of the two isomers of isopropylmalate. Q97W36 Q97W36 2.3.3.13 2-isopropylmalate synthase. 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating). Alpha-IPM synthetase. Alpha-isopropylmalate synthase. Alpha-isopropylmalate synthetase. Alpha-isopropylmalic synthetase. Isopropylmalate synthase. Isopropylmalate synthetase. Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA. K(+). -!- Formerly EC 4.1.3.12. Q97W70 Q97W70 2.7.1.39 Homoserine kinase. ATP + L-homoserine = ADP + O-phospho-L-homoserine. Q97WE6 Q97WE6 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). Q97XW1 Q97XW1 2.7.1.30 Glycerol kinase. ATP:glycerol 3-phosphotransferase. Glycerokinase. ATP + glycerol = ADP + sn-glycerol 3-phosphate. -!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. Q97YJ9 Q97YJ9 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. Q97ZF0 Q97ZF0 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. Q97ZK9 Q97ZK9 6.1.1.9 Valine--tRNA ligase. Valine translase. Valyl-tRNA synthetase. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Q97ZT9 Q97ZT9 7.3.2.1 ABC-type phosphate transporter. ABC phosphate transporter. Phosphate-transporting ATPase. ATP + H(2)O + phosphate-[phosphate-binding protein](Side 1) = ADP + phosphate + phosphate(Side 2) + [phosphate-binding protein](Side 1). -!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of phosphate anions. -!- Unlike P-type ATPases, it does not undergo phosphorylation during the transport process. -!- Formerly EC 3.6.3.27. Q97ZX0 Q97ZX0 6.1.1.2 Tryptophan--tRNA ligase. L-tryptophan-tRNA(Trp) ligase (AMP-forming). TrpRS. Tryptophan translase. Tryptophanyl ribonucleic synthetase. Tryptophanyl-transfer ribonucleate synthetase. Tryptophanyl-transfer ribonucleic acid synthetase. Tryptophanyl-transfer ribonucleic synthetase. Tryptophanyl-transfer RNA synthetase. Tryptophanyl-tRNA synthase. Tryptophanyl-tRNA synthetase. ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl- tRNA(Trp). Q97ZY3 Q97ZY3 4.6.1.16 tRNA-intron lyase. PretRNA lyase (intron-removing; cyclic-2',3'-phosphate-forming). tRNA splicing endonuclease. PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus. -!- The enzyme catalyzes the final stage in the maturation of tRNA molecules. -!- Formerly EC 3.1.27.9. Q97ZZ8 Q97ZZ8 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). Q97ZZ8 Q97ZZ8 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. Q980A0 Q980A0 5.4.2.12 Phosphoglycerate mutase (2,3-diphosphoglycerate-independent). 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Cofactor independent phosphoglycerate mutase. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. Cobalt cation or Mn(2+). -!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. Q980I5 Q980I5 2.5.1.19 3-phosphoshikimate 1-carboxyvinyltransferase. 3-enol-pyruvoylshikimate-5-phosphate synthase. 5-enolpyruvylshikimate-3-phosphate synthase. EPSP synthase. Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate. Q980I7 Q980I7 4.2.3.5 Chorismate synthase. 5-enolpyruvylshikimate-3-phosphate phospholyase. 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. FMN. -!- The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). -!- Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. -!- Formerly EC 4.6.1.4. Q980L3 Q980L3 6.1.1.21 Histidine--tRNA ligase. Histidine translase. Histidyl-tRNA synthetase. ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). Q980L7 Q980L7 2.4.2.48 tRNA-guanine(15) transglycosylase. Transfer ribonucleic acid guanine(15) transglycosylase. tRNA guanine(15) transglycosidase. Guanine(15) in tRNA + 7-cyano-7-carbaguanine = 7-cyano-7-carbaguanine(15) in tRNA + guanine. -!- Archaeal tRNAs contain the modified nucleoside archaeosine at position 15. -!- This archaeal enzyme catalyzes the exchange of guanine at position 15 of tRNA with the base preQ(0), which is ultimately modified to form the nucleoside archaeosine (cf. EC 2.6.1.97). Q980P7 Q980P7 6.3.4.23 Formate--phosphoribosylaminoimidazolecarboxamide ligase. 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase. 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase. ATP + formate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = ADP + phosphate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide. -!- This archaeal enzyme, characterized from the methanogen Methanocaldococcus jannaschii, catalyzes a step in the synthesis of purine nucleotides. -!- It differs from the orthologous bacterial/eukaryotic enzymes, which utilize 10-formyltetrahydrofolate rather than formate and ATP. -!- Cf. EC 2.1.2.3. Q980Q4 Q980Q4 2.4.2.9 Uracil phosphoribosyltransferase. UMP diphosphorylase. UMP pyrophosphorylase. UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. Q980R2 Q980R2 2.7.7.6 DNA-directed RNA polymerase. DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48. Q980U7 Q980U7 1.2.1.70 Glutamyl-tRNA reductase. L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. -!- Forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway, which is used in most eubacteria, and in all archaebacteria, algae and plants. -!- However, in the alpha-proteobacteria EC 2.3.1.37 is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. -!- This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. -!- Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. Q980V2 Q980V2 5.4.99.27 tRNA pseudouridine(13) synthase. tRNA Psi(13) synthase. tRNA uridine(13) = tRNA pseudouridine(13). -!- Pseudouridine synthase PusS from Escherichia coli specifically acts on uridine(13) in tRNA. -!- The Pus7 protein from Saccharomyces cerevisiae is a multisite- multisubstrate pseudouridine synthase that is able to modify uridine(13) in several yeast tRNAs, uridine(35) in the pre-tRNA(Tyr), uridine(35) in U2 small nuclear RNA, and uridine(50) in 5S rRNA. Q9ADK0 Q9ADK0 3.5.1.115 Mycothiol S-conjugate amidase. A mycothiol S-conjugate + H(2)O = an N-acetyl L-cysteine-S-conjugate + 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol. -!- The enzyme that is found in actinomycetes is involved in the detoxification of oxidizing agents and electrophilic antibiotics. -!- The enzyme has low activity with 1-O-(2-acetamido-2-deoxy-alpha-D- glucopyranosyl)-1D-myo-inositol as substrate (cf. EC 3.5.1.103). Q9CDL9 Q9CDL9 6.3.1.2 Glutamine synthetase. Glutamate--ammonia ligase. L-glutamine synthetase. ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. -!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements. Q9CE78 Q9CE78 6.1.1.21 Histidine--tRNA ligase. Histidine translase. Histidyl-tRNA synthetase. ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). Q9CEF5 Q9CEF5 2.7.11.1 Non-specific serine/threonine protein kinase. Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase. ATP + a protein = ADP + a phosphoprotein. -!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70. Q9CEX2 Q9CEX2 6.1.1.11 Serine--tRNA ligase. Serine translase. SerRS. Seryl-transfer ribonucleate synthetase. Seryl-transfer ribonucleic acid synthetase. Seryl-transfer RNA synthetase. Seryl-tRNA synthetase. (1) ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). (2) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). -!- This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1. Q9CG49 Q9CG49 6.2.1.54 D-alanine--[D-alanyl-carrier protein] ligase. ATP + D-alanine + holo-[D-alaninyl-carrier protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier protein]. -!- The enzyme is involved in the modification of wall teichoic acids, as well as type I and IV lipoteichoic acids, with D-alanine residues. -!- It activates D-alanine using ATP to form a high-energy (D-alanyl)adenylate intermediate and subsequently transfers the alanyl moiety to the phosphopantheinyl prosthetic group of a D-alanyl-carrier protein (DltC). Q9CGD4 Q9CGD4 7.6.2.11 ABC-type polyamine transporter. Polyamine ABC transporter. Polyamine-transporting ATPase. ATP + H(2)O + polyamine-[polyamine-binding protein](Side 1) = ADP + phosphate + polyamine(Side 2) + [polyamine-binding protein](Side 1). -!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- Does not undergo phosphorylation during the transport process. -!- A bacterial enzyme that imports putrescine and spermidine. -!- In Escherichia coli the enzyme imports spermidine preferentially. -!- Formerly EC 3.6.3.31. Q9CH12 Q9CH12 5.4.2.7 Phosphopentomutase. Deoxyribomutase. Deoxyribose phosphomutase. Phosphodeoxyribomutase. Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. -!- Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D- ribose 5-phosphate. -!- Alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5- bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.6. Q9CID9 Q9CID9 5.4.2.10 Phosphoglucosamine mutase. Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. -!- The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. -!- The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6- bisphosphate, which is an intermediate in the reaction, alpha-D- glucose 1,6-bisphosphate or ATP. -!- It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. Q9CIH5 Q9CIH5 6.1.1.1 Tyrosine--tRNA ligase. L-tyrosine-tRNA(Tyr) ligase (AMP-forming). Tyrosine translase. Tyrosine tRNA synthetase. Tyrosine-transfer ribonucleate synthetase. Tyrosine-transfer RNA ligase. Tyrosyl-transfer ribonucleate synthetase. Tyrosyl-transfer ribonucleic acid synthetase. Tyrosyl-transfer RNA synthetase. Tyrosyl-tRNA ligase. Tyrosyl-tRNA synthetase. ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). Q9CIM0 Q9CIM0 5.4.2.11 Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). 2,3-diphosphoglycerate dependent phosphoglycerate mutase. Cofactor dependent phosphoglycerate mutase. PGAM. Phosphoglycerate phosphomutase. Phosphoglyceromutase. 2-phospho-D-glycerate = 3-phospho-D-glycerate. -!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1. Q9CIW1 Q9CIW1 2.7.2.3 Phosphoglycerate kinase. ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. Q9FBM1 Q9FBM1 1.17.7.4 4-hydroxy-3-methylbut-2-enyl diphosphate reductase. (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase. HMBPP reductase. (1) Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). (2) Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). Iron-sulfur. -!- Forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. -!- This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. -!- This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. -!- The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate. -!- Formerly EC 1.17.1.2. Q9FCA6 Q9FCA6 1.14.19.69 Biflaviolin synthase. CYP158A2. (1) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,3'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O. (2) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,8'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O. -!- This cytochrome-P450 (heme-thiolate) enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyzes a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product. -!- The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation. -!- Formerly EC 1.14.21.7. Q9HT18 Q9HT18 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q9HTJ2 Q9HTJ2 1.1.99.1 Choline dehydrogenase. Choline oxidase. Choline-cytochrome c reductase. Choline + acceptor = betaine aldehyde + reduced acceptor. Pyrroloquinoline quinone. -!- In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyze the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. -!- In plants, the first reaction is catalyzed by EC 1.14.15.7 whereas in animals and many bacteria, it is catalyzed by either EC 1.1.99.1 or EC 1.1.3.17. -!- The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria. Q9HTJ2 Q9HTJ2 1.2.1.8 Betaine-aldehyde dehydrogenase. BADH. Betaine aldehyde dehydrogenase. Betaine aldehyde oxidase. Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH. -!- In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. -!- This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. -!- In contrast, different enzymes are involved in the first reaction. -!- In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17. -!- In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157. Q9HU05 Q9HU05 5.4.99.5 Chorismate mutase. Hydroxyphenylpyruvate synthase. Chorismate = prephenate. Q9HUF4 Q9HUF4 2.7.7.42 [Glutamine synthetase] adenylyltransferase. [Glutamate--ammonia-ligase] adenylyltransferase. Glutamate-ammonia-ligase adenylyltransferase. Glutamine-synthetase adenylyltransferase. ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine. -!- This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89). -!- The two activities are present on separate domains. Q9HUF4 Q9HUF4 2.7.7.89 [Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase. [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP. -!- This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42). -!- The two activities are present on separate domains. -!- Formerly EC 3.1.4.15. Q9HUF7 Q9HUF7 2.7.10.2 Non-specific protein-tyrosine kinase. Cytoplasmic protein tyrosine kinase. ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. -!- Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain. -!- In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families. -!- Formerly EC 2.7.1.112. Q9HUJ2 Q9HUJ2 4.1.99.17 Phosphomethylpyrimidine synthase. 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO. Iron-sulfur. -!- Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. -!- The first stage of catalysis is reduction of the S-adenosyl-L- methionine to produce L-methionine and a 5'-deoxyadenosin-5'-yl radical that is crucial for the conversion of the substrate. -!- Part of the pathway for thiamine biosynthesis. Q9HUK1 Q9HUK1 5.6.2.3 DNA topoisomerase (ATP-hydrolyzing). DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase. ATP-dependent breakage, passage and rejoining of double-stranded DNA. -!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3. Q9HVW9 Q9HVW9 1.1.1.23 Histidinol dehydrogenase. L-histidinol + H(2)O + 2 NAD(+) = L-histidine + 2 NADH. -!- Also oxidizes L-histidinal. -!- The Neurospora enzyme also catalyzes the reactions of EC 3.5.4.19 and EC 3.6.1.31. Q9HVZ9 Q9HVZ9 6.3.2.9 UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase. D-glutamate ligase. D-glutamate-adding enzyme. MurD synthetase. UDP-Mur-NAC-L-Ala:D-Glu ligase. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase. UDP-N-acetylmuramoylalanine--D-glutamate ligase. Uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase. ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate. -!- Involved in the synthesis of a cell-wall peptide in bacteria. Q9HXU0 Q9HXU0 6.1.1.6 Lysine--tRNA ligase. Lysine translase. Lysyl-tRNA synthetase. ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). Q9HY65 Q9HY65 2.6.1.87 UDP-4-amino-4-deoxy-L-arabinose aminotransferase. UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase. UDP-4-amino-4-deoxy-L-arabinose aminomutase. UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase. UDP-Ara4O aminotransferase. UDP-L-Ara4N transaminase. UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate = UDP-beta-L-threo- pentapyranos-4-ulose + L-glutamate. Pyridoxal 5'-phosphate. -!- Formerly EC 2.6.1.n1. Q9HZK8 Q9HZK8 7.2.1.1 NADH:ubiquinone reductase (Na(+)-transporting). Na(+)-NQR. Na(+)-translocating NADH-quinone reductase. NADH + ubiquinone + n Na(+)(In) = NAD(+) + ubiquinol + n Na(+)(Out). FAD; FMN; Iron-sulfur; Riboflavin. -!- An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster. -!- Formerly EC 1.6.5.8. Q9HZP8 Q9HZP8 1.3.1.9 Enoyl-[acyl-carrier-protein] reductase (NADH). Enoyl-ACP reductase. NADH-enoyl acyl carrier protein reductase. NADH-specific enoyl-ACP reductase. An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH. -!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons. Q9HZP8 Q9HZP8 1.3.1.44 Trans-2-enoyl-CoA reductase (NAD(+)). Acyl-CoA + NAD(+) = trans-didehydroacyl-CoA + NADH. -!- The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA. Q9I099 Q9I099 6.1.1.3 Threonine--tRNA ligase. Threonine translase. Threonyl-tRNA synthetase. ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). Q9I4G3 Q9I4G3 1.9.6.1 Nitrate reductase (cytochrome). 2 ferrocytochrome + nitrate + 2 H(+) = 2 ferricytochrome + nitrite. Q9KWU4 Q9KWU4 6.4.1.1 Pyruvate carboxylase. Pyruvic carboxylase. ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate. Biotin; Mn(2+) or Zn(2+). -!- The animal enzyme requires acetyl-CoA. Q9KWZ1 Q9KWZ1 2.5.1.72 Quinolinate synthase. Quinolinate synthetase. Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate. Iron-sulfur. -!- Quinolinate synthase catalyzes the second step in the de novo biosynthesis of NAD(+) from aspartate in some bacteria, with EC 1.4.3.16 catalyzing the first step and EC 2.4.2.19 the third step. -!- In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme. Q9KY56 Q9KY56 6.2.1.5 Succinate--CoA ligase (ADP-forming). Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming). ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. Q9KZK8 Q9KZK8 6.3.2.31 Coenzyme F420-0:L-glutamate ligase. GTP + coenzyme F420-0 + L-glutamate = GDP + phosphate + coenzyme F420-1. -!- This protein catalyzes the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. -!- In the reaction described here the enzyme attaches a glutamate via its alpha-amine group to F420-0. -!- In the second reaction (EC 6.3.2.34) it catalyzes the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate. Q9KZK8 Q9KZK8 6.3.2.34 Coenzyme F420-1:gamma-L-glutamate ligase. GTP + coenzyme F420-1 + L-glutamate = GDP + phosphate + coenzyme gamma- F420-2. -!- This protein catalyzes the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. -!- In the first reaction (EC 6.3.2.31) the enzyme attaches a glutamate via its alpha-amine group to F420-0. -!- In the second reaction, which is described here, the enzyme catalyzes the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate. Q9L0Q6 Q9L0Q6 6.1.1.16 Cysteine--tRNA ligase. Cysteine translase. Cysteinyl-tRNA synthetase. ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). Q9PHN5 Q9PHN5 1.1.1.86 Ketol-acid reductoisomerase (NADP(+)). Acetohydroxy acid isomeroreductase. Alpha-keto-beta-hydroxylacyl reductoisomerase. Dihydroxyisovalerate dehydrogenase (isomerizing). (1) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2- methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2- ethyl-3-oxobutanoate + NADPH. -!- The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383). -!- Formerly EC 1.1.1.89. Q9PIB8 Q9PIB8 2.5.1.55 3-deoxy-8-phosphooctulonate synthase. 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating). 2-dehydro-3-deoxy-phosphooctonate aldolase. 2-keto-3-deoxy-8-phosphooctonic synthetase. 3-deoxy-D-manno-octulosonate-8-phosphate synthase. 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase. 3-deoxy-D-mannooctulosonate-8-phosphate synthetase. 3-deoxyoctulosonic 8-phosphate synthetase. KDO-8-P synthase. KDO-8-phosphate synthetase. KDOP synthase. Phospho-2-keto-3-deoxyoctonate aldolase. Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 3-deoxy-D-manno- octulosonate 8-phosphate + phosphate. -!- Formerly EC 4.1.2.16. Q9PIB9 Q9PIB9 2.5.1.78 6,7-dimethyl-8-ribityllumazine synthase. Lumazine synthase. 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6- (D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H(2)O + phosphate. -!- Involved in riboflavin biosynthesis. Q9PLV4 Q9PLV4 1.7.1.13 PreQ(1) synthase. 7-cyano-7-deazaguanine reductase. PreQ(0) oxidoreductase. PreQ(0) reductase. 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-carbaguanine + 2 NADPH. -!- The reaction occurs in the reverse direction. -!- This enzyme catalyzes one of the early steps in the synthesis of queosine (Q-tRNA), and is followed by the action of EC 2.4.2.29. -!- Queosine is found in the wobble position of tRNA(GUN) in eukaryotes and bacteria and is thought to be involved in translational modulation. Q9PPE0 Q9PPE0 1.11.1.15 Peroxiredoxin. AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. Q9RGG4 Q9RGG4 2.7.1.206 Protein-N(pi)-phosphohistidine--L-sorbose phosphotransferase. L-sorbose PTS permease. [Protein]-N(pi)-phospho-L-histidine + L-sorbose(Side 1) = [protein]-L- histidine + L-sorbose 1-phosphate(Side 2). -!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69. Q9RJH9 Q9RJH9 1.11.1.21 Catalase peroxidase. (1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O. -!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. Q9RQQ9 Q9RQQ9 2.7.13.3 Histidine kinase. Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. -!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor. Q9S5G6 Q9S5G6 2.6.1.9 Histidinol-phosphate transaminase. Histidinol-phosphate aminotransferase. Imidazole acetol-phosphate transaminase. Imidazolylacetolphosphate aminotransferase. L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. Pyridoxal 5'-phosphate. Q9UWX2 Q9UWX2 6.1.1.15 Proline--tRNA ligase. Proline translase. Prolyl-tRNA synthetase. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). Q9UX04 Q9UX04 1.3.1.14 Dihydroorotate dehydrogenase (NAD(+)). DHOD. DHODase. DHOdehase. Dihydroorotate oxidase. Orotate reductase (NADH(2)). Orotate reductase (NADH). (S)-dihydroorotate + NAD(+) = orotate + NADH. FAD; FMN; Iron-sulfur. -!- The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit. -!- The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. -!- Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP(+) (EC 1.3.1.15) as electron acceptor. -!- The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor. Q9UX10 Q9UX10 4.1.1.23 Orotidine-5'-phosphate decarboxylase. OMP decarboxylase. OMPdcase. Orotidine-5'-phosphate carboxy-lyase. Orotidylic decarboxylase. UMP synthase. Uridine 5'-monophosphate synthase. Orotidine 5'-phosphate = UMP + CO(2). -!- The enzyme from higher eukaryotes is identical with EC 2.4.2.10. Q9UX20 Q9UX20 6.3.2.6 Phosphoribosylaminoimidazolesuccinocarboxamide synthase. 4-((N-succinylamino)carbonyl)-5-aminoimidazole ribonucleotide synthetase. 4-(N-succinocarboxamide)-5-aminoimidazole synthetase. 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase. Phosphoribosylaminoimidazole-succinocarboxamide synthase. Phosphoribosylaminoimidazole-succinocarboxamide synthetase. Phosphoribosylaminoimidazolesuccinocarboxamide synthetase. SAICAR synthase. SAICAR synthetase. SAICARs. ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate. -!- Forms part of the purine biosynthesis pathway. Q9UX24 Q9UX24 6.3.5.3 Phosphoribosylformylglycinamidine synthase. FGAM synthase. FGAM synthetase. FGAR amidotransferase. FGARAT. Formylglycinamide ribotide amidotransferase. Phosphoribosylformylglycinamidine synthetase. ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine + L-glutamate. Q9UX31 Q9UX31 6.3.4.5 Argininosuccinate synthase. Arginine succinate synthetase. Argininosuccinate synthetase. Citrulline--aspartate ligase. ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate. Q9UXB1 Q9UXB1 6.1.1.5 Isoleucine--tRNA ligase. Isoleucine translase. Isoleucyl-tRNA synthetase. ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl- tRNA(Ile). Q9UXG1 Q9UXG1 3.6.4.12 DNA helicase. ATP + H(2)O = ADP + phosphate. -!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase). Q9V2V5 Q9V2V5 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. Q9V2V6 Q9V2V6 3.4.25.1 Proteasome endopeptidase complex. Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome. Cleavage of peptide bonds with very broad specificity. -!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46. Q9X8I3 Q9X8I3 3.5.4.16 GTP cyclohydrolase I. GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate. -!- The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. -!- Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12. Q9XA14 Q9XA14 3.4.22.70 Sortase A. The enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. -!- Belongs to peptidase family C60. Q9Z3S1 Q9Z3S1 3.1.1.31 6-phosphogluconolactonase. 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-phospho-D-gluconate. Q9Z687 Q9Z687 7.1.2.2 H(+)-transporting two-sector ATPase. ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase. ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2). -!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14. Q9ZGI2 Q9ZGI2 2.3.1.239 10-deoxymethynolide syntase. (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (10-deoxymethynolide forming). Malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH = 10-deoxymethynolide + 6 CoA + 6 CO(2) + 5 NADP(+) + 2 H(2)O. -!- The product, 10-deoxymethynolide, contains a 12-membered ring and is an intermediate in the biosynthesis of methymycin in the bacterium Streptomyces venezuelae. -!- The enzyme also produces narbonolide (see EC 2.3.1.240). -!- The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. -!- Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). -!- Not all active sites are used in the biosynthesis. Q9ZGI2 Q9ZGI2 2.3.1.240 Narbonolide synthase. Pikromycin PKS. Malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH = narbonolide + 7 CoA + 7 CO(2) + 5 NADP(+) + 2 H(2)O. -!- The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae. -!- The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239). -!- The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. -!- Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). -!- Not all active sites are used in the biosynthesis. Q9ZGI3 Q9ZGI3 2.3.1.239 10-deoxymethynolide syntase. (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (10-deoxymethynolide forming). Malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH = 10-deoxymethynolide + 6 CoA + 6 CO(2) + 5 NADP(+) + 2 H(2)O. -!- The product, 10-deoxymethynolide, contains a 12-membered ring and is an intermediate in the biosynthesis of methymycin in the bacterium Streptomyces venezuelae. -!- The enzyme also produces narbonolide (see EC 2.3.1.240). -!- The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. -!- Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). -!- Not all active sites are used in the biosynthesis. Q9ZGI3 Q9ZGI3 2.3.1.240 Narbonolide synthase. Pikromycin PKS. Malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH = narbonolide + 7 CoA + 7 CO(2) + 5 NADP(+) + 2 H(2)O. -!- The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae. -!- The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239). -!- The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. -!- Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). -!- Not all active sites are used in the biosynthesis. Q9ZNH4 Q9ZNH4 4.1.1.49 Phosphoenolpyruvate carboxykinase (ATP). PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase. ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2).