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| | mtnW | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase (DK-MTP-1-P enolase); Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1- phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate (HK-MTPenyl-1-P); Belongs to the RuBisCO large chain family. Type IV subfamily. (405 aa) |
| | rocR | Transcriptional regulator (NtrC/NifA family); Positive regulator of arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF and probably acts by binding to the corresponding upstream activating sequences. (461 aa) |
| | rocD | Ornithine aminotransferase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism. (401 aa) |
| | rocE | Arginine/ornithine/gamma-aminobutyrate permease; Putative transport protein involved in arginine degradative pathway. Probably transports arginine or ornithine. (467 aa) |
| | argI | Arginase; Involved in the catabolism of arginine. Belongs to the arginase family. (296 aa) |
| | asnH | Asparagine synthetase (glutamine-hydrolyzing); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparagine synthetase family. (747 aa) |
| | mmsA | Methylmalonate-semialdehyde dehydrogenase; Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. (487 aa) |
| | iolD | 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase; Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG). (637 aa) |
| | yxeK | Putative monooxygenase; Probably catalyzes the oxygenation of the 2-position of the succinyl moiety of N-acetyl-S-(2-succino)cysteine, causing a spontaneous elimination reaction of the resulting hemithioketal that generates oxaloacetate and N-acetylcysteine (NAC). Is involved in a S- (2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. (441 aa) |
| | yxeL | Putative acetyltransferase; Catalyzes the N-acetylation of S-(2-succino)cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Moreover, 2SC is a toxic compound in B.subtilis at high exogenous concentrations, and this enzyme relieves 2SC toxicity via N-acetylation; Belongs to the acetyltransferase family. (165 aa) |
| | yxeP | Putative amidohydrolase; Probably catalyzes the deacetylation of N-acetylcysteine (NAC) to acetate and cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Belongs to the peptidase M20 family. (380 aa) |
| | hutG | Formiminoglutamate hydrolase; Catalyzes the conversion of N-formimidoyl-L-glutamate to L- glutamate and formamide. (319 aa) |
| | hutI | Imidazolone-5-propionate hydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (421 aa) |
| | hutU | Urocanase; Catalyzes the conversion of urocanate to 4-imidazolone-5- propionate; Belongs to the urocanase family. (552 aa) |
| | hutH | Histidine ammonia-lyase (histidase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (508 aa) |
| | hutP | Transcriptional antiterminator; Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization; Belongs to the HutP family. (148 aa) |
| | yxjG | Putative methyltetrahydrofolate methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To B.subtilis YxjH. (378 aa) |
| | yxjH | Putative methyl-tetrahydrofolate methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To B.subtilis YxjG. (377 aa) |
| | ilvK | Branched-chain amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (363 aa) |
| | tyrZ | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. (413 aa) |
| | rocG | Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...] (424 aa) |
| | rocA | Delta-1-pyrroline-5 carboxylate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (515 aa) |
| | rocB | Putative N-deacylase involved in arginine and ornithine utilization; Involved in arginine degradative pathway. (566 aa) |
| | rocC | Arginine/ornithine permease; Putative transport protein involved in arginine degradative pathway. Probably transports arginine or ornithine. (470 aa) |
| | thrZ | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family. (638 aa) |
| | speB | Agmatinase; Catalyzes the formation of putrescine from agmatine; Belongs to the arginase family. Agmatinase subfamily. (290 aa) |
| | argS | arginyl-tRNA synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (556 aa) |
| | pyrG | CTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (535 aa) |
| | glyA | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity); Belongs to the SHMT family. (415 aa) |
| | alsS | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (570 aa) |
| | hisZ | histidyl-tRNA synthetase-like component of ATP phophoribosyltransferase; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity). (391 aa) |
| | hisG | ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity); Belongs to the ATP phosphoribosyltransferase family. Short subfamily. (213 aa) |
| | hisD | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (427 aa) |
| | hisB | Imidazoleglycerol-phosphate dehydratase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (194 aa) |
| | hisH | Amidotransferase (glutaminase); IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity). (212 aa) |
| | hisA | Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (245 aa) |
| | hisF | Imidazole glycerol phosphate synthase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity). (252 aa) |
| | hisI | phosphoribosyl-AMP cyclohydrolase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; In the C-terminal section; belongs to the PRA-PH family. (209 aa) |
| | cysJ | Sulfite reductase (flavoprotein alpha-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable). (605 aa) |
| | cysI | Sulfite reductase (hemoprotein beta-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (Probable); Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (571 aa) |
| | putM | Proline dehydrogenase 1; Converts proline to delta-1-pyrroline-5-carboxylate. (302 aa) |
| | gcvH | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (127 aa) |
| | sufS | Cysteine desulfurase; Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40- to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. (406 aa) |
| | pucG | Vitamin B6-dependent (S)-ureidoglycine glyoxylate aminotransferase; Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. (416 aa) |
| | hom | Homoserine dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (433 aa) |
| | thrC | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa) |
| | thrB | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (309 aa) |
| | dapF | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. (284 aa) |
| | ald | L-alanine dehydrogenase; Catalyzes the reversible oxidative deamination of L-alanine to pyruvate. This enzyme is a key factor in the assimilation of L- alanine as an energy source through the tricarboxylic acid cycle during sporulation. (378 aa) |
| | patB | Promiscuous cystathionine beta-lyase / cysteine desulfhydrase; Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily. (387 aa) |
| | yugH | Putative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (386 aa) |
| | asnB | Asparagine synthetase; Main asparagine synthetase in vegetative cells. (632 aa) |
| | leuS | leucyl-tRNA synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (804 aa) |
| | ytkP | Putative cysteine synthase-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (311 aa) |
| | aroX | 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I DAHP synthase family. (358 aa) |
| | tyrS | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). (422 aa) |
| | hisJ | Histidinol phosphate phosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the PHP hydrolase family. HisK subfamily. (268 aa) |
| | argG | Argininosuccinate synthase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (403 aa) |
| | argH | Argininosuccinate lyase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (461 aa) |
| | thrS | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family. (643 aa) |
| | ysaA | Putative phosphatase; Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro; Belongs to the HAD-like hydrolase superfamily. (260 aa) |
| | pheS | phenylalanyl-tRNA synthetase (alpha subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (344 aa) |
| | pheT | phenylalanyl-tRNA synthetase (beta subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (804 aa) |
| | lysC | Aspartokinase II alpha subunit (aa 1->408) and beta subunit (aa 246->408); Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. (408 aa) |
| | ilvB | Acetolactate synthase (acetohydroxy-acid synthase) (large subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (574 aa) |
| | ilvH | Acetolactate synthase (acetohydroxy-acid synthase) (small subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acetolactate synthase small subunit family. (172 aa) |
| | ilvC | Acetohydroxy-acid isomeroreductase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. (342 aa) |
| | leuA | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (518 aa) |
| | leuB | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. (365 aa) |
| | leuC | 3-isopropylmalate dehydratase (large subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate; Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. (472 aa) |
| | leuD | 3-isopropylmalate dehydratase (small subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (199 aa) |
| | valS | valyl-tRNA synthetase; As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (By similarity). Catalyzes the attachment of valine to tRNA(Val); Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (880 aa) |
| | pheA | Prephenate dehydratase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (285 aa) |
| | nadB | L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate. (531 aa) |
| | nadA | Quinolinate synthetase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. (368 aa) |
| | dtd | D-Tyr-tRNATyr deacylase; A non-functional D-aminoacyl-tRNA deacylase. (132 aa) |
| | hisS | histidyl-tRNA synthetase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (424 aa) |
| | aspS | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (592 aa) |
| | alaS | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. (878 aa) |
| | mtnN | Methylthioadenosine / S-adenosylhomocysteine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Belongs to the PNP/UDP phosphorylase family. MtnN subfamily. (231 aa) |
| | mccA | Cystathionine beta-synthase for the reverse transsulfuration pathway; Catalyzes the conversion of O-acetylserine and homocysteine to cystathionine. (307 aa) |
| | mccB | Cystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide. (379 aa) |
| | gltR | Transcriptional regulator (LysR family); Positive regulator of glutamate biosynthesis (gltAB genes). Negatively regulates its own expression; Belongs to the LysR transcriptional regulatory family. (296 aa) |
| | aroD | Shikimate 5-dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). (280 aa) |
| | comER | Putative pyrroline-5'-carboxylate reductase; Dispensable for transformability. Not known if it can act as a pyrroline-5-carboxylate reductase. (273 aa) |
| | glyQ | glycyl-tRNA synthetase (alpha subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (295 aa) |
| | glyS | glycyl-tRNA synthetase (beta subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (679 aa) |
| | gcvT | Aminomethyltransferase (glycine cleavage system protein T); The glycine cleavage system catalyzes the degradation of glycine. (362 aa) |
| | gcvPA | Glycine decarboxylase (subunit 1) (glycine cleavage system protein P); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity). (448 aa) |
| | gcvPB | Glycine decarboxylase (subunit 2) (glycine cleavage system protein P); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity); Belongs to the GcvP family. C-terminal subunit subfamily. (488 aa) |
| | aroQ | 3-dehydroquinate dehydratase, type II; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (148 aa) |
| | folD | Methylenetetrahydrofolate dehydrogenase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. (283 aa) |
| | ahrC | Transcriptional regulator; Represses the synthesis of biosynthetic enzymes and activates the arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF. (149 aa) |
| | bcd | Branched-chain amino acid dehydrogenase; Catalyzes the reversible deamination of L-leucine to 4- methyl-2-oxopentanoate. (364 aa) |
| | bkdAA | Branched-chain alpha-keto acid dehydrogenase E1 subunit; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the BCKDHA family. (330 aa) |
| | bkdAB | Branched-chain alpha-keto acid dehydrogenase E1 subunit; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). (327 aa) |
| | yqjN | Putative N-deacylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To B.subtilis RocB. (547 aa) |
| | proI | Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (278 aa) |
| | dsdA | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. (448 aa) |
| | ansA | Exported L-asparaginase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparaginase 1 family. (329 aa) |
| | ansB | L-aspartase (aspartate ammonia lyase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II fumarase/aspartase family. Aspartase subfamily. (475 aa) |
| | lysA | Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (439 aa) |
| | aroC | 3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. Belongs to the type-I 3-dehydroquinase family. (255 aa) |
| | serA | 3-phosphoglycerate dehydrogenase; Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. (525 aa) |
| | gudB | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] (427 aa) |
| | aroF | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. (390 aa) |
| | aroB | 3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ); Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family. (362 aa) |
| | aroH | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. (127 aa) |
| | trpE | Anthranilate synthase; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of am [...] (515 aa) |
| | trpD | Indole-3-glycerol phosphate synthase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (338 aa) |
| | trpF | Phosphoribosyl anthranilate isomerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the TrpF family. (215 aa) |
| | trpB | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (400 aa) |
| | trpA | Tryptophan synthase (alpha subunit); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate; Belongs to the TrpA family. (267 aa) |
| | hisC | Histidinol-phosphate aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (360 aa) |
| | tyrA | Prephenate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the prephenate/arogenate dehydrogenase family. (371 aa) |
| | aroA | 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvoylshikimate-3-phosphate synthase); Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. (428 aa) |
| | dapB | (4S)-4-hydroxy-2,3,4, 5-tetrahydro-(2S)-dipicolinic acid (HTPA) dehydratase reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. (267 aa) |
| | panD | Aspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. (127 aa) |
| | asnS | asparaginyl-tRNA synthetase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (430 aa) |
| | metA | Putative homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. (301 aa) |
| | ilvD | Dihydroxy-acid dehydratase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the IlvD/Edd family. (558 aa) |
| | dfrA | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). (168 aa) |
| | ilvA | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity). (422 aa) |
| | kamA | Lysine 2,3-aminomutase; Catalyzes the interconversion of L-alpha-lysine and L-beta- lysine; Belongs to the radical SAM superfamily. KamA family. (471 aa) |
| | odhB | 2-oxoglutarate dehydrogenase complex (dihydrolipoamide transsuccinylase, E2 subunit); E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (417 aa) |
| | yobN | Putative amine oxidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the flavin monoamine oxidase family. FIG1 subfamily. (478 aa) |
| | yoaD | Putative 2-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (344 aa) |
| | proH | Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (297 aa) |
| | proJ | Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (371 aa) |
| | gltC | Transcriptional regulator (LysR family); Positive regulator of glutamate biosynthesis (gltAB genes). Negatively regulates its own expression. (300 aa) |
| | gltA | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. (1520 aa) |
| | gltB | Glutamate synthase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (493 aa) |
| | ppsA | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. (2561 aa) |
| | ppsE | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. (1279 aa) |
| | yngG | Putative hydroxymethylglutaryl-CoA lyase; Involved in the catabolism of branched amino acids such as leucine; Belongs to the HMG-CoA lyase family. (299 aa) |
| | yngE | Putative methylcrotonoyl-CoA carboxylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the AccD/PCCB family. (511 aa) |
| | alrB | Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (394 aa) |
| | glnA | Glutamine synthetase; Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA- binding active state and turns on the transcription of genes required for nitrogen assimilation. Under condi [...] (444 aa) |
| | tdh | Threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. (347 aa) |
| | dapA | Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (290 aa) |
| | dapG | Aspartokinase I (alpha and beta subunits); Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. Belongs to the aspartokinase family. (404 aa) |
| | asd | Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (346 aa) |
| | proS | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] (564 aa) |
| | cysH | (phospho)adenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. (233 aa) |
| | pyrAB | Pyrimidine-specific carbamoyl-phosphate synthetase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the CarB family. (1071 aa) |
| | pyrAA | Pyrimidine-specific carbamoyl-phosphate synthetase (small subunit, glutaminase subunit); Evidence 2b: Function of strongly homologous gene; enzyme. (364 aa) |
| | pyrB | Aspartate carbamoyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (304 aa) |
| | ileS | isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). (921 aa) |
| | glsB | Glutaminase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (309 aa) |
| | dapL | N-acetyl-diaminopimelate deacetylase; Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate. (374 aa) |
| | dapH | Tetrahydrodipicolinate N-acetyltransferase; Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate. (236 aa) |
| | dapX | N-acetyl-L,L-diaminopimelate aminotransferase; Essential for murein biosynthesis. Probably catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL- 2,6-diaminopimelate (Probable); Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (393 aa) |
| | mtnD | Acireductone dioxygenase (Ni2+ or Fe2+-requiring); Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway. (178 aa) |
| | mtnB | Methylthioribulose-1-phosphate dehydratase (MTRu-1-P dehydratase); Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Belongs to the aldolase class II family. MtnB subfamily. (209 aa) |
| | mtnX | 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphatephosphatase (HK-MTPenyl-1-P phosphatase); Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5- methylthiopentene (DHK-MTPene). (235 aa) |
| | mtnE | Methionine-glutamine aminotransferase; Catalyzes the formation of methionine from 2-keto-4- methylthiobutyrate (KMTB). (398 aa) |
| | mtnK | Methylthioribose kinase (methionine salvage pathway); Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate. (397 aa) |
| | mtnA | Methylthioribose-1-phosphate isomerase (methionine salvage pathway); Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). (353 aa) |
| | metE | Cobalamin-independent methionine synthase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation. (762 aa) |
| | proA | Gamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. (415 aa) |
| | proB | Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (365 aa) |
| | ykgA | Putative aminohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the DDAH family. (286 aa) |
| | proG | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (272 aa) |
| | metC | Cystathionine beta-lyase; Catalyzes the transformation of cystathionine into homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the trans-sulfuration enzymes family. (390 aa) |
| | metI | Cystathionine gamma-synthase and O-acetylhomoserine thiolyase; Catalyzes the formation of L-cystathionine from O-acetyl-L- homoserine and L-cysteine. Cannot use O-succinyl-L-homoserine as substrate. Also exhibits O-acetylhomoserine thiolyase activity, catalyzing the synthesis of L-homocysteine from O-acetyl-L-homoserine and sulfide. (373 aa) |
| | thiO | FAD-dependent glycine oxidase; Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N- methylglycine), N-ethylglycine and glycine. Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine. Does not act on L-amino acids and other D-amino acids. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine interm [...] (369 aa) |
| | trpS | tryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (330 aa) |
| | argF | Ornithine carbamoyltransferase; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family. (319 aa) |
| | carB | Arginine-specific carbamoyl-phosphate synthetase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the CarB family. (1030 aa) |
| | carA | Arginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (353 aa) |
| | argD | N-acetylornithine aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (385 aa) |
| | argB | N-acetylglutamate 5-phosphotransferase (acetylglutamate kinase); Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. (258 aa) |
| | argJ | Ornithine acetyltransferase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. (406 aa) |
| | argC | N-acetylglutamate gamma-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. (345 aa) |
| | samT | Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (612 aa) |
| | yitB | Putative phospho-adenylylsulfate sulfotransferase; Reduction of activated sulfate into sulfite; Belongs to the PAPS reductase family. CysH subfamily. (236 aa) |
| | yisV | Putative PLP-dependent transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (484 aa) |
| | asnO | Asparagine synthetase; Asparagine synthetase involved in sporulation. (614 aa) |
| | serC | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (359 aa) |
| | dat | D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essen [...] (282 aa) |
| | gatB | glutamyl-tRNA(Gln) amidotransferase (subunit B); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (476 aa) |
| | gatC | glutamyl-tRNA(Gln) amidotransferase (subunit C); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity); Belongs to the GatC family. (96 aa) |
| | yerI | Putative kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the pseudomonas-type ThrB family. (336 aa) |
| | yerD | Putative flavoenzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (525 aa) |
| | purF | Glutamine phosphoribosylpyrophosphate amidotransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (476 aa) |
| | purQ | Phosphoribosylformylglycinamidine synthetase I; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist [...] (227 aa) |
| | guaA | GMP synthetase; Catalyzes the synthesis of GMP from XMP. (513 aa) |
| | gabP | Gamma-aminobutyrate (GABA) permease; High-affinity uptake system for GABA. Functions also as a low-affinity proline importer; Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family. (469 aa) |
| | ydfD | Putative PLP-dependent transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (482 aa) |
| | alrA | D-alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (389 aa) |
| | gabD | Succinate-semialdehyde dehydrogenase; Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate. (462 aa) |
| | gabT | 4-aminobutyrate aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (436 aa) |
| | yclM | Aspartate kinase III; Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. (454 aa) |
| | yczE | N-terminal part of 4'-phosphopantetheinyl transferase (Surfactin synthetase-activating enzyme); Evidence 7: Gene remnant; Product type e: enzyme. (215 aa) |
| | ycxD | Putative PLP-dependent transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (444 aa) |
| | srfAC | Surfactin synthetase; Probably activates a leucine. (1275 aa) |
| | putC | 1-pyrroline-5-carboxylate dehydrogenase; Important for the use of proline as a sole carbon and energy source or a sole nitrogen source. (515 aa) |
| | putB | Proline oxidase; Converts proline to delta-1-pyrroline-5-carboxylate. Important for the use of proline as a sole carbon and energy source or a sole nitrogen source. (303 aa) |
| | aroK | Shikimate kinase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family. (186 aa) |
| | ansZ | L-asparaginase 2 (putative lipoprotein); Catalyzes the conversion of L-asparagine to L-aspartate and ammonium. (375 aa) |
| | glsA | Glutaminase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (327 aa) |
| | ybgG | Homocysteine methylase using (R,S)AdoMet; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (315 aa) |
| | ilvE | Ketomethiobutyrate-branched-chain/aromatic amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (356 aa) |
| | glmS | L-glutamine-D-fructose-6-phosphate amidotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (600 aa) |
| | cysS | cysteinyl-tRNA synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (466 aa) |
| | cysE | Serine acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS). (217 aa) |
| | gltX | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (483 aa) |
| | lysS | lysyl-tRNA synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. (499 aa) |
| | pabA | 4-amino-4-deoxychorismate synthase; Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. Also involved in the biosynthesis of anthranilate. (194 aa) |
| | pabB | 4-amino-4-deoxychorismate synthase (para-aminobenzoate synthase); Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. (470 aa) |
| | cysK | Cysteine synthase; Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR- CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression. (308 aa) |
| | yabJ | Aminoacrylate/iminopropionate hydrolase/deaminase; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis. May have a role in the purine metabolism; Belongs to the RutC family. (125 aa) |
| | metS | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. (664 aa) |
| | serS | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (425 aa) |
| | pdxT | Glutamine amidotransferase for pyridoxal phosphate synthesis; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (196 aa) |
| | pdxS | Glutamine amidotransferase for pyridoxal phosphate synthesis; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. (294 aa) |
