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| | scpB | methylmalonyl-CoA decarboxylase, biotin-independent; Catalyzes the decarboxylation of (R)-methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propanoate. (261 aa) |
| | ygeX | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] (398 aa) |
| | lysA | Diaminopimelate decarboxylase, PLP-binding; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate; Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily. (420 aa) |
| | mltA | Membrane-bound lytic murein transglycosylase A; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. (365 aa) |
| | csdA | Cysteine sulfinate desulfinase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, and transiently retains the released sulfur atom on a cysteine residue, in the form of a persulfide. Can also desulfinate L-cysteine sulfinate, which is the best substrate of the enzyme. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Seems to participate in Fe/S biogenesis by recruiting the SufBCD-SufE proteins. Transfers sulfur to CsdE that increases the cys [...] (401 aa) |
| | fucA | L-fuculose-1-phosphate aldolase; Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1- phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L- lactaldehyde (Ref.8, Ref.9,. Also able to catalyze the reversible cleavage of D- ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1- phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively. FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes and has [...] (215 aa) |
| | sdaB | L-serine dehydratase 2; Deaminates also threonine, particularly when it is present in high concentration; Belongs to the iron-sulfur dependent L-serine dehydratase family. (455 aa) |
| | gudX | Glucarate dehydratase-related protein, substrate unknown; Does not seem to have an in-vivo activity on glucarate or idarate. Its real substrate is unknown. (446 aa) |
| | gudD | D-glucarate dehydratase 1; Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D- glucarate (5-kdGluc). Also acts on L-idarate; Belongs to the mandelate racemase/muconate lactonizing enzyme family. GlucD subfamily. (446 aa) |
| | eno | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, [...] (432 aa) |
| | queE | 7-carboxy-7-deazaguanine synthase; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (223 aa) |
| | queD | 6-pyruvoyl tetrahydrobiopterin synthase (PTPS); Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP. (121 aa) |
| | ispF | 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). Also converts 4-diphosphocytidyl-2-C-methyl-D- erythritol into 2-C-methyl-D-erythritol 3,4-cyclophosphate and CMP. (159 aa) |
| | ygbL | Putative class II aldolase; Catalyzes the decarboxylation of 3-oxo-tetronate 4-phosphate to dihydroxyacetone phosphate (DHAP) and CO(2). Belongs to the aldolase class II family. AraD/FucA subfamily. (212 aa) |
| | hypE | Carbamoyl dehydratase, hydrogenases 1,2,3 maturation protein; Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group. The cyano group is then transferred from HypE to the HypC-HypD complex or the HybG-HypD complex. (336 aa) |
| | mltB | Membrane-bound lytic murein transglycosylase B; Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division. (361 aa) |
| | luxS | S-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. (171 aa) |
| | pheA | Chorismate mutase and prephenate dehydratase, P-protein; Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. (386 aa) |
| | mltF | Membrane-bound lytic transglycosylase F, murein hydrolase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. (518 aa) |
| | dapA | Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). Belongs to the DapA family. (292 aa) |
| | eutB | Ethanolamine ammonia-lyase, heavy chain; Protein involved in amine catabolic process. (453 aa) |
| | eutC | Ethanolamine ammonia-lyase, small subunit (light chain); Ethanolamine ammonia-lyase, light chain; Protein involved in amine catabolic process; Belongs to the EutC family. (295 aa) |
| | murQ | N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase; Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate. Is required for growth on MurNAc as the sole source of carbon and energy. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. (298 aa) |
| | cysK | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] (323 aa) |
| | oxc | Oxalyl CoA decarboxylase, ThDP-dependent; Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA; Belongs to the TPP enzyme family. (564 aa) |
| | dsdA | D-serine dehydratase (deaminase); Protein involved in cellular amino acid catabolic process. (442 aa) |
| | fadJ | enoyl-CoA hydratase/epimerase and isomerase/3-hydroxyacyl-CoA dehydrogenase; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (714 aa) |
| | aroC | 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. It uses NADPH to reduce FMN. (361 aa) |
| | menH | 2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase; Catalyzes a proton abstraction reaction that results in 2,5- elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Is also able to catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in vitro; Belongs to the AB hydrolase superfamily. MenH family. (252 aa) |
| | menB | Dihydroxynaphthoic acid synthetase; Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2- naphthoyl-CoA (DHNA-CoA). (285 aa) |
| | menC | O-succinylbenzoyl-CoA synthase; Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- carboxylate (SHCHC) to 2-succinylbenzoate (OSB). (320 aa) |
| | rhmD | L-rhamnonate dehydratase; Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Can also dehydrate L-lyxonate, L-mannonate and D- gulonate, although less efficiently, but not 2-keto-4-hydroxyheptane- 1,7-dioate; Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily. (401 aa) |
| | rhmA | 2-keto-3-deoxy-L-rhamnonate aldolase; Catalyzes the reversible retro-aldol cleavage of 2-keto-3- deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde. 2-keto-3-deoxy- L-mannonate, 2-keto-3-deoxy-L-lyxonate and 4-hydroxy-2-ketoheptane-1,7- dioate (HKHD) are also reasonably good substrates, although 2-keto-3- deoxy-L-rhamnonate is likely to be the physiological substrate. (267 aa) |
| | psuG | Pseudouridine 5'-phosphate glycosidase; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. (312 aa) |
| | fbaB | Fructose-bisphosphate aldolase class I; Protein involved in glycolysis; Belongs to the DeoC/FbaB aldolase family. FbaB subfamily. (350 aa) |
| | gatY | D-tagatose 1,6-bisphosphate aldolase 2, catalytic subunit; Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol. (284 aa) |
| | gmd | GDP-D-mannose dehydratase, NAD(P)-binding; Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6- deoxy-D-mannose; Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily. (373 aa) |
| | rfbB | dTDP-glucose 4,6 dehydratase, NAD(P)-binding; Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6- deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction; Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily. (361 aa) |
| | hisF | Imidazole glycerol phosphate synthase, catalytic subunit with HisH; 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; Belongs to the HisA/HisF family. (258 aa) |
| | hisH | Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; 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. (196 aa) |
| | hisB | Imidazoleglycerolphosphate dehydratase and histidinol-phosphate phosphatase; Protein involved in histidine biosynthetic process. (355 aa) |
| | hchA | Protein/nucleic acid deglycase 1; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, [...] (283 aa) |
| | dcyD | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. (328 aa) |
| | edd | 6-phosphogluconate dehydratase; Catalyzes the dehydration of 6-phospho-D-gluconate to 2- dehydro-3-deoxy-6-phospho-D-gluconate. (603 aa) |
| | eda | KHG/KDPG aldolase; Involved in the degradation of glucose via the Entner- Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D- glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile. (213 aa) |
| | sdaA | L-serine dehydratase 1; Deaminates also threonine, particularly when it is present in high concentration; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa) |
| | aroD | 3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids (AroAA). Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsylon-amino group of a lys-170 at the active site. (252 aa) |
| | sufS | Cysteine desulfurase, stimulated by SufE; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd [...] (406 aa) |
| | ydhZ | Uncharacterized protein; In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate. (69 aa) |
| | gloA | Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. (135 aa) |
| | nth | DNA glycosylase and apyrimidinic (AP) lyase (endonuclease III); DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. (211 aa) |
| | malY | PLP-dependent beta-cystathionase and maltose regulon regulator; Acts as a beta-cystathionase and as a repressor of the maltose regulon. (390 aa) |
| | fumA | Fumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. (548 aa) |
| | fumC | Fumarate hydratase (fumarase C),aerobic Class II; Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress. Catalyzes the stereospecific interconversion of fumarate to L-malate. Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (467 aa) |
| | gadB | Glutamate decarboxylase B, PLP-dependent; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria; Belongs to the group II decarboxylase family. (466 aa) |
| | paaG | 1,2-epoxyphenylacetyl-CoA isomerase, oxepin-CoA-forming; Catalyzes the reversible conversion of the epoxide to 2- oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA). (262 aa) |
| | paaF | 2,3-dehydroadipyl-CoA hydratase; Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA. Belongs to the enoyl-CoA hydratase/isomerase family. (255 aa) |
| | paaZ | oxepin-CoA hydrolase and 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase; Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)- ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C- terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6- dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6- dehydrosuberyl-CoA. Can also use crotonyl-CoA [...] (681 aa) |
| | pyrF | Orotidine-5'-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). (245 aa) |
| | acnA | Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript. (891 aa) |
| | trpE | Component I of 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 conce [...] (520 aa) |
| | trpD | Anthranilate phosphoribosyltransferase; 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 con [...] (531 aa) |
| | trpC | Indole-3-glycerolphosphate synthetase and N-(5-phosphoribosyl)anthranilate isomerase; Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. (453 aa) |
| | trpB | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine; Belongs to the TrpB family. (397 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. (268 aa) |
| | chaC | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. (231 aa) |
| | emtA | Lytic murein endotransglycosylase E; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain. Prefers cross-linked murein in vivo; Belongs to the transglycosylase Slt family. (203 aa) |
| | purB | Adenylosuccinate lyase; Protein involved in purine nucleotide biosynthetic process; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. (456 aa) |
| | yceG | Septation protein, ampicillin sensitivity; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family. (340 aa) |
| | pabC | 4-amino-4-deoxychorismate lyase component of para-aminobenzoate synthase multienzyme complex; Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (269 aa) |
| | mgsA | Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. (152 aa) |
| | fabA | Beta-hydroxydecanoyl thioester dehydrase; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. (172 aa) |
| | ycaC | Putative isochorismatase family hydrolase; Protein involved in cellular amino acid catabolic process. (208 aa) |
| | ltaE | L-allo-threonine aldolase, PLP-dependent; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro- phenylserine are also good substrates. (333 aa) |
| | fsaA | Fructose-6-phosphate aldolase 1; Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)- threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, s [...] (220 aa) |
| | ybiW | Putative pyruvate formate lyase; Probably shows dehydratase activity. Belongs to the glycyl radical enzyme (GRE) family. (810 aa) |
| | moaC | Molybdopterin biosynthesis, protein C; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). (161 aa) |
| | moaA | Molybdopterin biosynthesis protein A; Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). (329 aa) |
| | nei | Endonuclease VIII and 5-formyluracil/5-hydroxymethyluracil DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Acts on DNA bubble and 3'-fork structures, suggesting a role in replication- associated DNA repair. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a sing [...] (263 aa) |
| | phr | Deoxyribodipyrimidine photolyase, FAD-binding; Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. (472 aa) |
| | speF | Ornithine decarboxylase isozyme, inducible; Protein involved in polyamine biosynthetic process; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (732 aa) |
| | rlpA | Septal ring protein, suppressor of prc, minor lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides; Belongs to the RlpA family. (362 aa) |
| | citE | Citrate lyase, citryl-ACP lyase (beta) subunit; Represents a citryl-ACP lyase. (302 aa) |
| | citF | Citrate lyase, citrate-ACP transferase (alpha) subunit; Represents a citrate:acetyl-ACP transferase. (510 aa) |
| | rna | Ribonuclease I; One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid. (268 aa) |
| | gcl | Glyoxylate carboligase; Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). (593 aa) |
| | allA | Ureidoglycolate lyase, releasing urea; Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the anaerobic utilization of allantoin as sole nitrogen source. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate. (160 aa) |
| | ybaK | Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase; Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. May compensate for the lack of Cys-tRNA(Pro) editing by ProRS. Is also able to deacylate Cys-tRNA(Cys), and displays weak deacylase activity in vitro against Gly-tRNA(Gly), as well as, at higher concentrations, some other correctly charged tRNAs. Unlike some of its orthologs it is not able to remove the amino acid moiety from incorrectly charged Ala- tRNA(Pro); Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (159 aa) |
| | hemH | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. (320 aa) |
| | hemB | 5-aminolevulinate 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; Belongs to the ALAD family. (324 aa) |
| | mhpE | 4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase, class I; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of 3-phenylpropanoate. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. (337 aa) |
| | mhpD | 2-keto-4-pentenoate hydratase; Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid. Belongs to the hydratase/decarboxylase family. MhpD subfamily. (269 aa) |
| | cynS | Cyanate aminohydrolase; Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. (156 aa) |
| | cynT | Carbonic anhydrase; Reversible hydration of carbon dioxide. Carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (CynS) diffuses out of the cell faster than it would be hydrated to bicarbonate, so the apparent function of this enzyme is to catalyze the hydration of carbon dioxide and thus prevent depletion of cellular bicarbonate. (219 aa) |
| | prpD | 2-methylcitrate dehydratase; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2- methyl-aconitate. It is also able to catalyze the dehydration of citrate and the hydration of cis-aconitate at a lower rate. Due to its broad substrate specificity, it seems to be responsible for the residual aconitase activity of the acnAB-null mutant. Belongs to the PrpD family. (483 aa) |
| | prpB | 2-methylisocitrate lyase; Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2- methylisocitrate to yield pyruvate and succinate via an alpha-carboxy- carbanion intermediate; Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family. (296 aa) |
| | yagF | CP4-6 prophage; Catalyzes the dehydration of D-xylonic acid to form 2- dehydro-3-deoxy-D-pentonate; Belongs to the IlvD/Edd family. (655 aa) |
| | yagE | 2-keto-3-deoxy gluconate (KDG) aldolase; Catalyzes the formation of 2-keto-3-deoxy-gluconate (KDG) from pyruvate and glyceraldehyde. May also function as a 2-dehydro-3-deoxy-D-pentonate aldolase. Overexpression leads to increased growth (over 2 hours) in the presence of the antibiotics norfloxacin, ampicillin and streptomycin ; Belongs to the DapA family. (302 aa) |
| | mltD | Putative membrane-bound lytic murein transglycosylase D; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity); Belongs to the transglycosylase Slt family. (452 aa) |
| | ldcC | Lysine decarboxylase 2, constitutive; Plays a role in lysine utilization by acting as a lysine decarboxylase. (713 aa) |
| | fabZ | (3R)-hydroxymyristol acyl carrier protein dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. (151 aa) |
| | panD | Aspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine; Belongs to the PanD family. (126 aa) |
| | can | Putative carbonic anhdrase; Belongs to the beta-class carbonic anhydrase family. (220 aa) |
| | speD | S-adenosylmethionine decarboxylase; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. (264 aa) |
| | acnB | Aconitate hydratase 2; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA- binding regulatory protein. During oxidative stress inactive AcnB apo- enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilize [...] (865 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. (466 aa) |
| | leuD | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (201 aa) |
| | caiD | carnitinyl-CoA dehydratase; Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. (261 aa) |
| | thrC | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction. (428 aa) |
| | fbaA | Fructose-bisphosphate aldolase, class II; 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. (359 aa) |
| | yggD | MtlR family putative transcriptional repressor; In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate; Belongs to the MtlR/FumE family. (169 aa) |
| | speA | Biosynthetic arginine decarboxylase, PLP-binding; Catalyzes the biosynthesis of agmatine from arginine. Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. (658 aa) |
| | mltC | Membrane-bound lytic murein transglycosylase C; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Belongs to the transglycosylase Slt family. (359 aa) |
| | speC | Ornithine decarboxylase, constitutive; Ornithine decarboxylase isozyme; Protein involved in polyamine biosynthetic process. (711 aa) |
| | metC | Cystathionine beta-lyase, PLP-dependent; Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis. Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine. In addition, under certain growth conditions, exhibits significant alanine racemase coactivity. (395 aa) |
| | ribB | 3,4-dihydroxy-2-butanone-4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. (217 aa) |
| | folB | Dihydroneopterin aldolase and dihydroneopterin triphosphate 2'-epimerase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6- hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin to dihydromonapterin at appreciable velocity; Belongs to the DHNA family. (122 aa) |
| | ttdA | L-tartrate dehydratase, subunit A; Protein involved in fermentation. (303 aa) |
| | ttdB | L-tartrate dehydratase, subunit B; Protein involved in fermentation. (201 aa) |
| | uxaA | Altronate hydrolase; Catalyzes the dehydration of D-altronate. (495 aa) |
| | tdcB | L-threonine dehydratase, catabolic; 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. TdcB also dehydrates serine t [...] (329 aa) |
| | garL | alpha-dehydro-beta-deoxy-D-glucarate aldolase; Catalyzes the reversible retro-aldol cleavage of both 5-keto- 4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde; Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase subfamily. (256 aa) |
| | garD | D-galactarate dehydrogenase; Catalyzes the dehydration of galactarate to form 5-dehydro-4- deoxy-D-glucarate. (523 aa) |
| | kbaY | Tagatose 6-phosphate aldolase 1, kbaY subunit; Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires KbaZ subunit for full activity and stability. (286 aa) |
| | elbB | Isoprenoid biosynthesis protein with amidotransferase-like domain; Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate. However, this apparent glyoxalase activity may reflect a protein deglycase activity, which could be the primary function of this protein like other DJ-1 superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is not able to use methylglyoxal as substrate. Belongs to the peptidase C56 family. (217 aa) |
| | nanA | N-acetylneuraminate lyase; Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate; Belongs to the DapA family. NanA subfamily. (297 aa) |
| | cysG | Uroporphyrinogen-III C-methyltransferase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. (457 aa) |
| | aroB | 3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). (362 aa) |
| | pck | Phosphoenolpyruvate carboxykinase [ATP]; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. Belongs to the phosphoenolpyruvate carboxykinase (ATP) family. (540 aa) |
| | gadA | Glutamate decarboxylase A, PLP-dependent; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. (466 aa) |
| | sgbH | 3-keto-L-gulonate 6-phosphate decarboxylase; Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. May be involved in the utilization of 2,3-diketo-L- gulonate. (220 aa) |
| | mutM | Formamidopyrimidine/5-formyluracil/ 5-hydroxymethyluracil DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:C, however it also acts on thymine glycol:G, 5,6-dihydrouracil:G and 5-hydroxyuracil:G. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-de [...] (269 aa) |
| | dfp | Coenzyme A biosynthesis bifunctional protein CoaBC; Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine. In the C-terminal section; belongs to the PPC synthetase family. (406 aa) |
| | tnaA | tryptophanase/L-cysteine desulfhydrase, PLP-dependent; Tryptophanase; Protein involved in cellular amino acid catabolic process; Belongs to the beta-eliminating lyase family. (471 aa) |
| | ilvD | Dihydroxyacid dehydratase. (616 aa) |
| | ilvA | L-threonine dehydratase, biosynthetic; 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. (514 aa) |
| | rffG | dTDP-glucose 4,6-dehydratase; Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6- deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction; Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily. (355 aa) |
| | hemD | Uroporphyrinogen III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. Belongs to the uroporphyrinogen-III synthase family. (246 aa) |
| | cyaA | Adenylate cyclase; Catalyzes the formation of the second messenger cAMP from ATP. Its transcript is probably degraded by endoribonuclease LS (rnlA), decreasing cAMP levels and the negative regulator Crp-cAMP, which then induces its own transcription again. (848 aa) |
| | ubiD | 3-octaprenyl-4-hydroxybenzoate decarboxylase; Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis; Belongs to the UbiD family. (497 aa) |
| | fadB | Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (729 aa) |
| | yihT | 6-deoxy-6-sulphofructose-1-phosphate aldolase; Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA). Belongs to the aldolase LacD family. (292 aa) |
| | rhaD | Rhamnulose-1-phosphate aldolase; Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. Also catalyzes the dephosphorylation of phospho- serine in vitro ; Belongs to the aldolase class II family. RhaD subfamily. (274 aa) |
| | fsaB | Fructose-6-phosphate aldolase 2; Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize hydroxyacetone as an alternative donor substrate. Is also able to catalyze the direct self-aldol addition of glycolaldehyde. Is less catalytically efficient than the isozyme FsaA. Does not display transaldolase activity. (220 aa) |
| | pflD | Putative glycine radical domain-containing pyruvate formate-lyase; Probably shows dehydratase activity. Belongs to the glycyl radical enzyme (GRE) family. (765 aa) |
| | ppc | Phosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. (883 aa) |
| | argH | Argininosuccinate lyase; Protein involved in arginine biosynthetic process. (457 aa) |
| | thiH | Tyrosine lyase, involved in thiamine-thiazole moiety synthesis; Catalyzes the radical-mediated cleavage of tyrosine to 2- iminoacetate and 4-cresol. (377 aa) |
| | thiC | Phosphomethylpyrimidine synthase; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. (631 aa) |
| | hemE | Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (354 aa) |
| | aceA | Isocitrate lyase; Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. (434 aa) |
| | ubiC | Chorismate pyruvate-lyase; Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. (165 aa) |
| | phnJ | Carbon-phosphorus lyase, SAM-dependent; Catalyzes the breakage of the C-P bond in alpha-D-ribose 1- methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic phosphate 5-phosphate (PRcP). (281 aa) |
| | adiA | Arginine decarboxylase; ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (755 aa) |
| | fumB | Anaerobic class I fumarate hydratase (fumarase B); Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate. Belongs to the class-I fumarase family. (548 aa) |
| | cadA | Lysine decarboxylase, acid-inducible; Inducible lysine decarboxylase that catalyzes the proton- dependent decarboxylation of L-lysine to produce the polyamine cadaverine and carbon dioxide. Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by- products of carbohydrate fermentation. Belongs to the Orn/Lys/Arg decarboxylase class-I family. (715 aa) |
| | aspA | Aspartate ammonia-lyase (aspartase); Protein involved in cellular amino acid metabolic process, asparagine biosynthetic process and lysine biosynthetic process via diaminopimelate. (478 aa) |
| | psd | Phosphatidylserine decarboxylase; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Only decarboxylates the lipid-linked form of the serine moiety, and not serine alone or derivatives like phosphoserine or glycerophosphoserine. (322 aa) |
| | nnr | Bifunctional NAD(P)H-hydrate repair enzyme; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. In the N-terminal section; belongs to the NnrE/AIBP family. (515 aa) |
| | ulaD | 3-keto-L-gulonate 6-phosphate decarboxylase; Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization. Belongs to the HPS/KGPDC family. KGPDC subfamily. (216 aa) |
| | yjhG | Putative dehydratase; Catalyzes the dehydration of D-xylonic acid to form 2- dehydro-3-deoxy-D-pentonate. (655 aa) |
| | yjhH | Putative lyase/synthase; Functions as a 2-dehydro-3-deoxy-D-pentonate aldolase. Belongs to the DapA family. (301 aa) |
| | uxuA | Mannonate hydrolase; Catalyzes the dehydration of D-mannonate. (394 aa) |
| | yjiM | Putative 2-hydroxyglutaryl-CoA dehydratase; Belongs to the FldB/FldC dehydratase alpha/beta subunit family. (383 aa) |
| | deoC | 2-deoxyribose-5-phosphate aldolase, NAD(P)-linked; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate. Can also catalyze the double aldol condensation of three acetaldehyde molecules, leading to the formation of 2,4,6-trideoxyhexose. Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily. (259 aa) |
| | slt | Lytic murein transglycosylase, soluble; Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division. (645 aa) |
| | tdcG | L-serine dehydratase; Protein involved in cellular amino acid catabolic process. (454 aa) |
| | dgoA | 2-oxo-3-deoxygalactonate 6-phosphate aldolase; Involved in the degradation of galactose via the DeLey- Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with re- facial selectivity. It can use a limited number of aldehyde substrates, including D-glyceraldehyde-3-phosphate (natural substrate), D- glyceraldehyde, glycolaldehyde, 2-pyridinecarboxaldehyde, D-ribose, D- erythr [...] (205 aa) |
| | dgoD | D-galactonate dehydratase; Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy- D-galactonate. (382 aa) |
