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prs prs cysK cysK cysE cysE ilvE ilvE aroK aroK hxlB hxlB hxlA hxlA yclM yclM citA citA yhdR yhdR serC serC asnO asnO samT samT argC argC argJ argJ argB argB argD argD argF argF metI metI metC metC proG proG proB proB proA proA metE metE dapX dapX dapH dapH dapL dapL pycA pycA rpe rpe sdaAB sdaAB sdaAA sdaAA asd asd dapG dapG dapA dapA glnA glnA tkt tkt citB citB gltB gltB gltA gltA proJ proJ proH proH yoaD yoaD yodQ yodQ ilvA ilvA ilvD ilvD metA metA aspB aspB dapB dapB aroA aroA tyrA tyrA hisC hisC trpA trpA trpB trpB trpF trpF trpD trpD trpE trpE aroH aroH aroB aroB aroF aroF serA serA aroC aroC lysA lysA proI proI mmgD mmgD aroQ aroQ aroD aroD mccB mccB mccA mccA mtnN mtnN yrrT yrrT pheA pheA yszB yszB leuD leuD leuC leuC leuB leuB leuA leuA ilvC ilvC ilvH ilvH ilvB ilvB lysC lysC gapB gapB icd icd citZ citZ pyk pyk pfkA pfkA argH argH argG argG hisJ hisJ aroX aroX ytkP ytkP ytjP ytjP asnB asnB metK metK luxS luxS patB patB dapF dapF thrB thrB thrC thrC hom hom eno eno pgm pgm tpiA tpiA pgk pgk gapA gapA hisI hisI hisF hisF hisA hisA hisH hisH hisB hisB hisD hisD hisG hisG hisZ hisZ alsS alsS glyA glyA ywlF ywlF ywjH ywjH fbaA fbaA ilvK ilvK asnH asnH argI argI
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prsPhosphoribosylpyrophosphate synthetase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P). (317 aa)
cysKCysteine 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)
cysESerine acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS). (217 aa)
ilvEKetomethiobutyrate-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)
aroKShikimate 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)
hxlB6-phospho-3-hexuloisomerase (PHI); Catalyzes the isomerization between 3-hexulose 6-phosphate and fructose 6-phosphate. Together with HxlA, may act as a formaldehyde detoxification system. (185 aa)
hxlA3-hexulose-6-phosphate synthase (HPS); Catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate. Together with HxlB, may act as a formaldehyde detoxification system; Belongs to the HPS/KGPDC family. HPS subfamily. (210 aa)
yclMAspartate 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)
citACitrate synthase I; Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect; Belongs to the citrate synthase family. (366 aa)
yhdRPutative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (393 aa)
serCPhosphoserine 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)
asnOAsparagine synthetase; Asparagine synthetase involved in sporulation. (614 aa)
samTBifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (612 aa)
argCN-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)
argJOrnithine 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)
argBN-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)
argDN-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)
argFOrnithine 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)
metICystathionine 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)
metCCystathionine 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)
proGRedundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (272 aa)
proBGlutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (365 aa)
proAGamma-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)
metECobalamin-independent methionine synthase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation. (762 aa)
dapXN-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)
dapHTetrahydrodipicolinate N-acetyltransferase; Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate. (236 aa)
dapLN-acetyl-diaminopimelate deacetylase; Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate. (374 aa)
pycAPyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second, leading to oxaloacetate production. Fulfills an anaplerotic function in B.subtilis as it is necessary for growth on glucose, but is not required for sporulation. (1148 aa)
rpeRibulose-5-phosphate 3-epimerase; Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate; Belongs to the ribulose-phosphate 3-epimerase family. (217 aa)
sdaABL-serine dehydratase (beta chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (220 aa)
sdaAAL-serine dehydratase (alpha chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (300 aa)
asdAspartate-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)
dapGAspartokinase 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)
dapADihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (290 aa)
glnAGlutamine 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)
tktTransketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. (667 aa)
citBAconitate hydratase (aconitase); Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the rehydration of 2- methyl-cis-aconitate to produce 2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the conce [...] (909 aa)
gltBGlutamate synthase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (493 aa)
gltAGlutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. (1520 aa)
proJGlutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (371 aa)
proHPyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (297 aa)
yoaDPutative 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)
yodQPutative deacylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (436 aa)
ilvAThreonine 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)
ilvDDihydroxy-acid dehydratase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the IlvD/Edd family. (558 aa)
metAPutative homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. (301 aa)
aspBPutative aspartate aminotransferase; 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 class-I pyridoxal-phosphate-dependent aminotransferase family. (393 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)
aroA3-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)
tyrAPrephenate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the prephenate/arogenate dehydrogenase family. (371 aa)
hisCHistidinol-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)
trpATryptophan 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)
trpBTryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (400 aa)
trpFPhosphoribosyl anthranilate isomerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the TrpF family. (215 aa)
trpDIndole-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)
trpEAnthranilate 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)
aroHChorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. (127 aa)
aroB3-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)
aroFChorismate 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)
serA3-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)
aroC3-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)
lysADiaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (439 aa)
proIPyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (278 aa)
mmgD2-methylcitrate synthase/citrate synthase III; Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Has both 2-methylcitrate synthase and citrate synthase activities. Catalyzes the condensation of propionyl-CoA and oxaloacetate to yield 2-methylcitrate (2-MC) and CoA, and the condensation of acetyl-CoA and oxaloacetate to yield citrate and CoA. Has 2.3-fold higher activity as a 2-methylcitrate synthase. Catalyzes the formation of either (2S,3R)- or (2R,3S)-2-methylcitrate. (372 aa)
aroQ3-dehydroquinate dehydratase, type II; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (148 aa)
aroDShikimate 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)
mccBCystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide. (379 aa)
mccACystathionine beta-synthase for the reverse transsulfuration pathway; Catalyzes the conversion of O-acetylserine and homocysteine to cystathionine. (307 aa)
mtnNMethylthioadenosine / 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)
yrrTPutative AdoMet-dependent methyltransferase; Could be a S-adenosyl-L-methionine-dependent methyltransferase; Belongs to the methyltransferase superfamily. YrrT family. (213 aa)
pheAPrephenate dehydratase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (285 aa)
yszBConserved hypothetical protein containing an ACT domain; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 2537815; Belongs to the UPF0735 family. (147 aa)
leuD3-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)
leuC3-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)
leuB3-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)
leuA2-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)
ilvCAcetohydroxy-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)
ilvHAcetolactate 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)
ilvBAcetolactate synthase (acetohydroxy-acid synthase) (large subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (574 aa)
lysCAspartokinase 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)
gapBGlyceraldehyde-3-phosphate dehydrogenase; Involved in the gluconeogenesis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3- bisphosphoglycerate (BPG) using the cofactor NADP. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NADP to NADPH. The reduced NADPH is then exchanged with the second NADP, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG; Belongs to the gl [...] (340 aa)
icdIsocitrate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (423 aa)
citZCitrate synthase II; Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect; Belongs to the citrate synthase family. (372 aa)
pykPyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family. (585 aa)
pfkA6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis; Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub- subfamily. (319 aa)
argHArgininosuccinate lyase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (461 aa)
argGArgininosuccinate 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)
hisJHistidinol 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)
aroX3-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)
ytkPPutative 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)
ytjPPutative dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (463 aa)
asnBAsparagine synthetase; Main asparagine synthetase in vegetative cells. (632 aa)
metKS-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (400 aa)
luxSS-ribosylhomocysteine lyase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD); Belongs to the LuxS family. (157 aa)
patBPromiscuous 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)
dapFDiaminopimelate 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)
thrBHomoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (309 aa)
thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa)
homHomoserine dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (433 aa)
enoEnolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. (430 aa)
pgmPhosphoglycerate mutase; Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (511 aa)
tpiATriose phosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (253 aa)
pgkPhosphoglycerate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the phosphoglycerate kinase family. (394 aa)
gapAGlyceraldehyde-3-phosphate dehydrogenase; Involved in the glycolysis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3- bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. (335 aa)
hisIphosphoribosyl-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)
hisFImidazole 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)
hisAPhosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (245 aa)
hisHAmidotransferase (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)
hisBImidazoleglycerol-phosphate dehydratase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (194 aa)
hisDHistidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (427 aa)
hisGATP 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)
hisZhistidyl-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)
alsSAlpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (570 aa)
glyASerine 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)
ywlFRibose 5-phosphate epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (149 aa)
ywjHPutative transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Does not show fructose-6-P aldolase activity. (212 aa)
fbaAFructose-1,6-bisphosphate aldolase; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. (285 aa)
ilvKBranched-chain amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (363 aa)
asnHAsparagine synthetase (glutamine-hydrolyzing); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparagine synthetase family. (747 aa)
argIArginase; Involved in the catabolism of arginine. Belongs to the arginase family. (296 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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