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| | prs | Phosphoribosylpyrophosphate 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) |
| | 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) |
| | cysE | Serine acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS). (217 aa) |
| | ycdF | Putative glucose 1-dehydrogenase; 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 short-chain dehydrogenases/reductases (SDR) family. (258 aa) |
| | ldh | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. (321 aa) |
| | nasF | uroporphyrin-III C-methyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the precorrin methyltransferase family. (483 aa) |
| | nasE | Assimilatory nitrite reductase subunit; Required for nitrite assimilation. Required for activity of the reductase (By similarity). (106 aa) |
| | nasD | Assimilatory nitrite reductase subunit; Required for nitrite assimilation. (805 aa) |
| | nasC | Assimilatory nitrate reductase (catalytic subunit); Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. (710 aa) |
| | nasB | Assimilatory nitrate reductase (electron transfer subunit NasB); Required for nitrate assimilation. (771 aa) |
| | hxlB | 6-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) |
| | hxlA | 3-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) |
| | bsdB | Phenolic acid decarboxylase subunit BsdB; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions. Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase (By similarity); Belongs to the UbiX/PAD1 family. YclB subfamily. (204 aa) |
| | bsdC | Phenolic acid decarboxylase subunit BsdC; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions. Phenolic acid decarboxylase that catalyzes the reversible decarboxylation of 4- hydroxybenzoate and vanillate. Could also catalyze the decarboxylation of salicylate (Probable). Is not active on di- and tri-hydroxybenzoate derivatives. Belongs to the UbiD family. YclC subfamily. (473 aa) |
| | bsdD | Phenolic acid decarboxylase subunit BsdD; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions, however the precise biochemical function of BsdD in metabolism of phenolic acid is unknown. (75 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) |
| | 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) |
| | gabD | Succinate-semialdehyde dehydrogenase; Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate. (462 aa) |
| | gdh | Glucose 1-dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (261 aa) |
| | cypD | Putative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS). (1061 aa) |
| | yfnB | Putative hydrolase; 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 HAD-like hydrolase superfamily. YjjG family. (235 aa) |
| | yfmT | Putative aldehyde dehydrogenase; A benzaldehyde dehydrogenase able to act on substrates with 3- and 4-hydroxy and methoxy substitutions; converts vanillin (4- hydroxy-3-methoxybenzaldehyde) to vanillic acid in vitro. The physiological substrate is unknown. (485 aa) |
| | yflL | Putative acylphosphatase; 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 acylphosphatase family. (91 aa) |
| | acoC | Acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (398 aa) |
| | acoL | Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (458 aa) |
| | catE | Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. (285 aa) |
| | gsaB | Glutamate-1-semialdehyde aminotransferase, class III aminotransferase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (429 aa) |
| | pgcA | Alpha-phosphoglucomutase; Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since glucose-1-phosphate is the precursor of UDP-glucose, which serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required fo [...] (581 aa) |
| | citA | Citrate 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) |
| | 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) |
| | yhfS | Putative acetyl-CoA C-acetyltransferase; May be involved in fatty acid metabolism; Belongs to the thiolase-like superfamily. Thiolase family. (364 aa) |
| | yisS | Putative myo-inositol 2-dehydrogenase; Catalyzes the reversible NAD(+)-dependent oxidation of scyllo-inositol (SI) to 2,4,6/3,5-pentahydroxycyclohexanone (scyllo- inosose or SIS). Is required for SI catabolism that allows B.subtilis to utilize SI as the sole carbon source for growth. Cannot use NADP(+) instead of NAD(+); Belongs to the Gfo/Idh/MocA family. (342 aa) |
| | yisZ | Putative adenylylsulfate kinase; Catalyzes the synthesis of activated sulfate. (199 aa) |
| | yitA | Putative sulfate adenylyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the sulfate adenylyltransferase family. (389 aa) |
| | yitB | Putative phospho-adenylylsulfate sulfotransferase; Reduction of activated sulfate into sulfite; Belongs to the PAPS reductase family. CysH subfamily. (236 aa) |
| | slpH | 2-phosphosulfolactate phosphatase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the ComB family. (228 aa) |
| | slpS | Phosphosulfolactate synthase; Catalyzes the addition of sulfite to phosphoenolpyruvate (PEP) to yield (2R)-phospho-3-sulfolactate (PSL) (By similarity). Is probably involved in the biosynthesis of L-sulfolactate, which is a major constituent of sporulating cells and mature spores. Belongs to the phosphosulfolactate synthase family. (252 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) |
| | 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) |
| | manP | Phosphotransferase system (PTS) mannose-specific enzyme IIBCA component; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannose transport. (650 aa) |
| | yjgC | Putative formate dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (985 aa) |
| | yjjA | Putative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (270 aa) |
| | pgl | 6-phosphogluconolactonase; Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. (349 aa) |
| | fruA | Phosphotransferase system (PTS) fructose-specific enzyme IIABC component; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in fructose transport. (635 aa) |
| | pdhA | Pyruvate dehydrogenase (E1 alpha subunit); The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). (371 aa) |
| | pdhB | Pyruvate dehydrogenase (E1 beta subunit); The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). (325 aa) |
| | pdhC | Pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit); The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). (442 aa) |
| | pdhD | Dihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (470 aa) |
| | pycA | Pyruvate 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) |
| | cysH | (phospho)adenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. (233 aa) |
| | sat | Sulfate adenylyltransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (382 aa) |
| | cysC | Adenylylsulfate kinase; Catalyzes the synthesis of activated sulfate; Belongs to the APS kinase family. (197 aa) |
| | sumT | Uroporphyrinogen III and precorrin-1 C-methyltransferase; Catalyzes both methylations at C-2 and C-7 of uroporphyrinogen III leading to precorrin-1 and precorrin-2; their oxidative esterification gives respectively factor I octamethyl ester and sirohydrochlorin. (257 aa) |
| | sirC | Precorrin-2 dehydrogenase; Catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin which is used as a precursor in both siroheme biosynthesis and in the anaerobic branch of adenosylcobalamin biosynthesis; Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. (162 aa) |
| | rpe | Ribulose-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) |
| | sucC | succinyl-CoA synthetase (beta subunit); Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (385 aa) |
| | sucD | succinyl-CoA synthetase (alpha subunit); Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (300 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) |
| | 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) |
| | dapA | Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (290 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) |
| | tkt | Transketolase; 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) |
| | citB | Aconitate 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) |
| | yngHA | Biotin carboxylase/methylcrotonoyl-CoA carboxylase subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (444 aa) |
| | galM | Aldose 1-epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the aldose epimerase family. (325 aa) |
| | gltB | Glutamate synthase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (493 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) |
| | 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) |
| | yoaI | Putative 4-hydroxyphenylacetate-3-hydroxylase; Catalyzes the hydroxylation of 4-hydroxyphenylacetic acid (4HPA), leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA). (483 aa) |
| | dhaS | Putative aldehyde dehydrogenase; 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 aldehyde dehydrogenase family. (495 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) |
| | odhA | 2-oxoglutarate dehydrogenase (E1 subunit); E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). (944 aa) |
| | kdgA | 2-keto-3-deoxygluconate-6-phosphate aldolase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (196 aa) |
| | kdgK | 2-keto-3-deoxygluconate kinase; Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Belongs to the carbohydrate kinase PfkB family. (324 aa) |
| | mgsA | Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. (137 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) |
| | 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) |
| | 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) |
| | lysA | Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (439 aa) |
| | zwf | Glucose-6-phosphate 1-dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. (489 aa) |
| | gndA | NADP+-dependent 6-P-gluconate dehydrogenase; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate. (469 aa) |
| | yqjD | Putative propionyl-CoA carboxylase beta chain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (507 aa) |
| | yqjC | Putative methylmalonyl-CoA epimerase; 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 methylmalonyl-CoA epimerase family. (140 aa) |
| | lpdV | Branched-chain alpha-keto acid dehydrogenase E3 subunit (dihydrolipoamide dehydrogenase); 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 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (474 aa) |
| | mmgD | 2-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) |
| | mmgB | 3-hydroxybutyryl-CoA dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (287 aa) |
| | mmgA | Degradative acetoacetyl-CoA thiolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (393 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) |
| | accC | acetyl-CoA carboxylase subunit (biotin carboxylase subunit); This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (450 aa) |
| | accB | acetyl-CoA carboxylase subunit (biotin carboxyl carrier subunit); This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA (By similarity). Binds biotin. (159 aa) |
| | glcK | Glucose kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the ROK (NagC/XylR) family. (321 aa) |
| | yqeC | Putative hydroxyacid dehydrogenase; May act as NAD-dependent 6-P-gluconate dehydrogenase. (297 aa) |
| | adhB | Putative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (378 aa) |
| | adhA | Putative dehydrogenase; Functions in the protection against aldehyde-stress. Belongs to the zinc-containing alcohol dehydrogenase family. (349 aa) |
| | cypB | Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. (1054 aa) |
| | yrhE | Putative formate dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; In the C-terminal section; belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (980 aa) |
| | yrbE | Putative oxidoreductase; 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 Gfo/Idh/MocA family. (341 aa) |
| | hemL | Glutamate-1-semialdehyde 2,1-aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (430 aa) |
| | hemB | Delta-aminolevulinic acid dehydratase (porphobilinogen synthase); Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). (324 aa) |
| | hemD | Uroporphyrinogen III cosynthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. Belongs to the uroporphyrinogen-III synthase family. (262 aa) |
| | hemC | Porphobilinogen deaminase (hydroxymethylbilane synthase); Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (314 aa) |
| | hemA | glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (455 aa) |
| | sdhB | Succinate dehydrogenase (iron-sulfur protein); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (253 aa) |
| | sdhA | Succinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (586 aa) |
| | sdhC | Succinate dehydrogenase (cytochrome b558 subunit); Di-heme cytochrome of the succinate dehydrogenase complex. (202 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) |
| | fadB | enoyl-CoA hydratase; Involved in the degradation of long-chain fatty acids. (258 aa) |
| | glcD | Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. (470 aa) |
| | glcF | Glycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. (444 aa) |
| | araD | L-ribulose-5-phosphate 4-epimerase; Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5- phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction). (229 aa) |
| | gapB | Glyceraldehyde-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) |
| | mdh | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa) |
| | icd | Isocitrate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (423 aa) |
| | citZ | Citrate 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) |
| | pyk | Pyruvate 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) |
| | pfkA | 6-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) |
| | accA | acetyl-CoA carboxylase (carboxyltransferase alpha subunit); Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. Belongs to the AccA family. (325 aa) |
| | accD | acetyl-CoA carboxylase (carboxyltransferase beta subunit); Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. (290 aa) |
| | nrnA | Oligoribonuclease (nanoRNAse), 3',5'-bisphosphate nucleotidase; Bifunctional enzyme which has both oligoribonuclease and pAp- phosphatase activities. Degrades RNA and DNA oligonucleotides with a length of 5 nucleotides and shorter, with a preference for 3-mers. Directionality is controversial; shown to degrade 5-mers and less in a 3' to 5' direction , and 11-mers in a 5' to 3' direction. Converts 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. (313 aa) |
| | ackA | Acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Appears to favor the formation of acetate. Involved in the secretion of excess carbohydrate. (395 aa) |
| | ytcI | Putative acyl-coenzyme A synthetase; 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 ATP-dependent AMP-binding enzyme family. (529 aa) |
| | acsA | acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA (By similarity). Has a role in growth and sporulation on acetate. (572 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) |
| | ytjP | Putative dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (463 aa) |
| | pckA | Phosphoenolpyruvate carboxykinase; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. (527 aa) |
| | yulF | Enzyme involved in biofilm formation; Catalyzes the NADPH-dependent reduction of scyllo-inosose (SIS) to scyllo-inositol (SI) in vitro, but is unable to dehydrogenate scyllo-inositol and myo-inositol. Is less efficient than the functional paralog IolW. Under physiological conditions, may primarily function as an NADPH-dependent oxidoreductase that reduces carbonyl group(s) in its substrates. Cannot use NADH instead of NADPH. (328 aa) |
| | rhaA | L-rhamnose isomerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the rhamnose isomerase family. (424 aa) |
| | rhaB | Rhamnulokinase; Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1- hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. Belongs to the rhamnulokinase family. (485 aa) |
| | pgi | Glucose-6-phosphate isomerase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the GPI family. (450 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) |
| | 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) |
| | thrC | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa) |
| | hom | Homoserine dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (433 aa) |
| | yutF | Putative p-nitrophenyl phosphatase; Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro; Belongs to the HAD-like hydrolase superfamily. NagD family. (256 aa) |
| | pucH | Allantoinase; Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (446 aa) |
| | pucL | Urate oxidase with peroxide reductase N-terminal domain; Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5- ureidoimidazoline (OHCU) to (S)-allantoin. (494 aa) |
| | pucM | 5-hydroxyisourate hydrolase; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). (114 aa) |
| | pucE | Xanthine dehydrogenase, iron-sulfur subunit; Oxidizes hypoxanthine and xanthine to uric acid. (173 aa) |
| | pucD | Xanthine dehydrogenase, substrate and molybdenum cofactor subunit; Oxidizes hypoxanthine and xanthine to uric acid. Belongs to the xanthine dehydrogenase family. (745 aa) |
| | pucC | Xanthine dehydrogenase, FAD-binding subunit; Oxidizes hypoxanthine and xanthine to uric acid. (277 aa) |
| | pucB | Enzyme for molybdopterin cofactor synthesis required for xanthine dehydrogenase; Required for xanthine dehydrogenase activity. Could be involved in formation of the molybdenum cofactor required by xanthine dehydrogenase. (205 aa) |
| | pucA | Xanthine dehydrogenase molybdopterin recruitment factor; Oxidizes hypoxanthine and xanthine to uric acid. PucA subunit could exert a molybdenum cofactor recruiting function. (330 aa) |
| | pucF | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S- ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (By similarity). (412 aa) |
| | fadA | acetyl-CoA C-acyltransferase; Involved in the degradation of long-chain fatty acids; Belongs to the thiolase-like superfamily. Thiolase family. (391 aa) |
| | fadN | enoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (789 aa) |
| | fumC | Fumarate hydratase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (462 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) |
| | 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) |
| | yvaA | Putative oxidoreductase; Catalyzes the reversible NADPH-dependent reduction of scyllo- inosose (SIS) to scyllo-inositol (SI). Cannot use NADH instead of NADPH. May be involved in reduction of not only SIS but also various oxidized compounds manifested upon stressful conditions. (358 aa) |
| | eno | Enolase; 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) |
| | pgm | Phosphoglycerate mutase; Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (511 aa) |
| | tpiA | Triose 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) |
| | pgk | Phosphoglycerate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the phosphoglycerate kinase family. (394 aa) |
| | gapA | Glyceraldehyde-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) |
| | yvcT | 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. (325 aa) |
| | yvkC | Putative phosphotransferase; 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 PEP-utilizing enzyme family. (831 aa) |
| | ureC | Urease (alpha subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family. (569 aa) |
| | ureB | Urease (beta subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the urease beta subunit family. (124 aa) |
| | ureA | Urease (gamma subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the urease gamma subunit family. (105 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) |
| | ywlF | Ribose 5-phosphate epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (149 aa) |
| | ywjI | Putative fructose 1,6-bisphosphatase class II; Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Can functionally substitute for the FBPase class 3 (Fbp) of B.subtilis. (321 aa) |
| | ywjH | Putative transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Does not show fructose-6-P aldolase activity. (212 aa) |
| | fbaA | Fructose-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) |
| | narI | Nitrate reductase (gamma subunit); The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. (223 aa) |
| | narH | Nitrate reductase (beta subunit); The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. (487 aa) |
| | narG | Nitrate reductase (alpha subunit); The alpha chain is the actual site of nitrate reduction. (1228 aa) |
| | ywhB | 1,3-keto-enol tautomerase; Catalyzes both 1,3- and 1,5-keto-enol tautomerization of the diacid 2-hydroxymuconate (2-hydroxy-2,4-hexadienedioate) to produce 2- oxo-4-hexenedioate. This reaction is highly stereoselective and produces a mixture of stereoisomers, where the (3S)-isomer of 2-oxo-4- hexenedioate predominates. Also catalyzes the tautomerization of 2- hydroxymuconate to 2-oxo-3-hexenedioate, however this reaction is slower and occurs after the tautomerization of 2-hydroxymuconate to 2- oxo-4-hexenedioate. Using 2-hydroxy-2,4-pentadienoate, phenylenolpyruvate, (p-hydroxyphenyl)- [...] (62 aa) |
| | pta | Phosphotransacetylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (323 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) |
| | ywdH | Putative aldehyde dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (456 aa) |
| | aldY | Putative aldehyde dehydrogenase; May contribute to protect cells against stress due to ethanol and related compounds; Belongs to the aldehyde dehydrogenase family. (485 aa) |
| | iolJ | 2-deoxy-5-keto-D-gluconic acid 6-phosphate aldolase; Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6- phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily. (290 aa) |
| | iolI | Inosose isomerase; Involved in the reversible interconverion of 2-keto-myo- inositol (2KMI, inosose or 2,4,6/3,5-pentahydroxycyclohexanone) to 1- keto-D-chiro-inositol (1KDCI or 2,3,5/4,6-pentahydroxycyclohexanone). Belongs to the IolI family. (278 aa) |
| | iolG | Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase; Involved in the oxidation of myo-inositol (MI) and D-chiro- inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D- chiro-inositol (1KDCI), respectively. Can also use D-glucose and D- xylose, and shows a trace of activity with D-ribose and D-fructose. (344 aa) |
| | iolE | 2-keto-myo-inositol dehydratase; Catalyzes the dehydration of inosose (2-keto-myo-inositol, 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol). (297 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) |
| | iolC | 2-deoxy-5-keto-D-gluconic acid kinase; Catalyzes the phosphorylation of 5-dehydro-2-deoxy-D- gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2- deoxy-D-gluconate (DKGP). (325 aa) |
| | iolB | 5-deoxy-D-glucuronic acid isomerase; Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate). (271 aa) |
| | aldX | Putative aldehyde dehydrogenase; 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 aldehyde dehydrogenase family. (445 aa) |
| | glxK | Glycerate kinase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (382 aa) |
| | gntK | Gluconate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (513 aa) |
| | gntZ | NAD+-6-phosphogluconate dehydrogenase; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to NADH. Does not contribute to oxidative pentose phosphate (PP) pathway fluxes during growth on glucose. The functional role of GntZ remains obscure. (468 aa) |
| | fbp | Fructose-1,6-bisphosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (641 aa) |
| | yycR | Putative dehydrogenase; 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 zinc-containing alcohol dehydrogenase family. (408 aa) |
