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| | iscU | Iron-sulfur cluster assembly scaffold protein; A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D- state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters; Belongs to the NifU family. (128 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) |
| | ydiJ | Putative FAD-linked oxidoreductase; Putative oxidase. (1018 aa) |
| | ydiO | Putative acyl-CoA dehydrogenase; Putative oxidoreductase; Belongs to the acyl-CoA dehydrogenase family. (383 aa) |
| | ydiR | Putative electron transfer flavoprotein, FAD-binding subunit; May play a role in a redox process; Belongs to the ETF alpha-subunit/FixB family. (312 aa) |
| | fadK | Short chain acyl-CoA synthetase, anaerobic; Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids. Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor. Can fun [...] (548 aa) |
| | astE | Succinylglutamate desuccinylase; Transforms N(2)-succinylglutamate into succinate and glutamate; Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily. (322 aa) |
| | astB | Succinylarginine dihydrolase; Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)- succinylornithine, ammonia and CO(2). (447 aa) |
| | astD | Succinylglutamic semialdehyde dehydrogenase; Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. Also shows activity with decanal or succinic semialdehyde as the electron donor and NAD as the electron acceptor. No activity is detected with NADP as the electron acceptor. Therefore, is an aldehyde dehydrogenase with broad substrate specificity. (492 aa) |
| | astA | Arginine succinyltransferase; Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. (344 aa) |
| | astC | Succinylornithine transaminase, PLP-dependent; Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily. (406 aa) |
| | ansA | Cytoplasmic L-asparaginase 1; Protein involved in cellular amino acid catabolic process; Belongs to the asparaginase 1 family. (338 aa) |
| | fadD | acyl-CoA synthetase (long-chain-fatty-acid--CoA ligase); Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms. Is involved in the aerobic beta- oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source. (561 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) |
| | edd | 6-phosphogluconate dehydratase; Catalyzes the dehydration of 6-phospho-D-gluconate to 2- dehydro-3-deoxy-6-phospho-D-gluconate. (603 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) |
| | gnd | 6-phosphogluconate dehydrogenase, decarboxylating; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. (468 aa) |
| | atoB | acetyl-CoA acetyltransferase; Protein involved in fatty acid oxidation. (394 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) |
| | pta | Phosphate acetyltransferase; Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. In the N-terminal section; belongs to the CobB/CobQ family. (714 aa) |
| | yfcF | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. (214 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) |
| | fadI | beta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. 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. Belongs to the thiolase-like superfamily. Thiolase family. (436 aa) |
| | dsdA | D-serine dehydratase (deaminase); Protein involved in cellular amino acid catabolic process. (442 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) |
| | frc | formyl-CoA transferase, NAD(P)-binding; 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 transfer of the CoA moiety from formyl- CoA to oxalate. It can also use succinate as an acceptor. (416 aa) |
| | cysM | Cysteine synthase B (O-acetylserine sulfhydrolase B); Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. (303 aa) |
| | murR | Repressor for murPQ, MurNAc 6-P inducible; Represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc). Binds to two adjacent inverted repeats within the operator region. MurNAc 6- phosphate, the substrate of MurQ, is the specific inducer that weakens binding of MurR to the operator. Also represses its own transcription. (285 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) |
| | iscS | Cysteine desulfurase (tRNA sulfurtransferase), PLP-dependent; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to a [...] (404 aa) |
| | hcaE | 3-phenylpropionate dioxygenase, large (alpha) subunit; Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. (453 aa) |
| | hcaF | 3-phenylpropionate dioxygenase, small (beta) subunit; Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. (172 aa) |
| | hcaC | 3-phenylpropionate dioxygenase, ferredoxin subunit; Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. This protein seems to be a 2Fe-2S ferredoxin. (106 aa) |
| | hcaB | 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Converts 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol) into 3-(2,3- dihydroxylphenyl)propanoic acid (DHPP) and 2,3-dihydroxicinnamic acid (DHCI), respectively; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (270 aa) |
| | hcaD | Phenylpropionate dioxygenase, ferredoxin reductase subunit; Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively; Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. (400 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. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...] (417 aa) |
| | grcA | Autonomous glycyl radical cofactor; Acts as a radical domain for damaged PFL and possibly other radical proteins. (127 aa) |
| | csiD | tRNA-Ile; Acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG) in the stationary phase of E.coli. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2- hydroxyglutarate. Other dicarboxylic acids (oxalate, malonate, succinate, adipate, and pimelate) are not substrates for this enzyme. (325 aa) |
| | lhgO | L-2-hydroxyglutarate oxidase; Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (422 aa) |
| | gabD | Succinate-semialdehyde dehydrogenase I, NADP-dependent; Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth. Also catalyzes the conversion of glutarate semialdehyde to glutarate, as part of a L- lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (482 aa) |
| | gabT | 4-aminobutyrate aminotransferase, PLP-dependent; Pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and glutamate. Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth. Also catalyzes the conversion of 5-aminovalerate to glutarate semialdehyde, as part of a L-lysine degradation pathway that proceeds via cadaverine, [...] (426 aa) |
| | gabP | Gamma-aminobutyrate transporter; Transporter for GABA; Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family. (466 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) |
| | 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) |
| | 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) |
| | 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) |
| | csdE | CsdA-binding activator; Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not appear to participate in Fe/S biogenesis; Belongs to the SufE family. (147 aa) |
| | kduD | 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase; Catalyzes the reversible reduction of 2,5-diketo-3- deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto- 3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH. To a lesser extent, can also reduce 5-keto- D-gluconate and oxidize D-gluconate and 1,2-propanediol. Together with KduI, seems to play a role in the catabolism of hexuronates under osmotic stress conditions, substituting for the regular hexuronate degrading enzymes UxaABC and UxuAB whose expression is repressed in these condition [...] (253 aa) |
| | kduI | Hexuronate isomerase; Catalyzes the isomerization of 5-dehydro-4-deoxy-D- glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate (By similarity). Plays a role in the catabolism of hexuronates under osmotic stress conditions, likely substituting for the regular hexuronate degrading enzyme UxaC whose expression is repressed in these conditions ; Belongs to the KduI family. (278 aa) |
| | yqeF | Short chain acyltransferase; Putative acyltransferase; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa) |
| | yqeA | Putative kinase; Belongs to the carbamate kinase family. (310 aa) |
| | gcvP | Glycine decarboxylase, PLP-dependent, subunit P of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. (957 aa) |
| | gcvH | Glycine cleavage complex lipoylprotein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (129 aa) |
| | gcvT | Aminomethyltransferase, tetrahydrofolate-dependent, subunit (T protein) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. (364 aa) |
| | 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) |
| | 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) |
| | ansB | Periplasmic L-asparaginase 2; Protein involved in cellular amino acid catabolic process; Belongs to the asparaginase 1 family. (348 aa) |
| | glcB | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA. (723 aa) |
| | glcD | Glycolate oxidase subunit, FAD-linked; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is required for E.coli to grow on glycolate as a sole source of carbon. Is also able to oxidize D-lactate ((R)-lactate) with a similar rate. 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. (499 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) |
| | patA | Putrescine:2-oxoglutaric acid aminotransferase, PLP-dependent; Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4- aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cad [...] (459 aa) |
| | fadH | 2,4-dienoyl-CoA reductase, NADH and FMN-linked; Functions as an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids with double bonds at even carbon positions. Catalyzes the NADPH-dependent reduction of the C4-C5 double bond of the acyl chain of 2,4-dienoyl-CoA to yield 2-trans-enoyl-CoA. Acts on both isomers, 2-trans,4- cis- and 2-trans,4-trans-decadienoyl-CoA, with almost equal efficiency. Is not active with NADH instead of NADPH. Does not show cis->trans isomerase activity. (672 aa) |
| | uxaA | Altronate hydrolase; Catalyzes the dehydration of D-altronate. (495 aa) |
| | uxaC | Uronate isomerase; Protein involved in carbohydrate catabolic process; Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family. (470 aa) |
| | yhaO | Putative transporter; Plays a role in L-cysteine detoxification. May transport both D- and L-serine (By similarity). Belongs to the amino acid/polyamine transporter 2 family. SdaC/TdcC subfamily. (443 aa) |
| | tdcF | Putative reactive intermediate deaminase; May be a post-translational regulator that controls the metabolic fate of L-threonine or the potentially toxic intermediate 2- ketobutyrate. (129 aa) |
| | tdcE | Pyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily. (764 aa) |
| | tdcD | Propionate kinase/acetate kinase C, anaerobic; Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor; Belongs to the acetokinase family. TdcD subfamily. (402 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) |
| | tdcA | Tdc operon transcriptional activator; Transcriptional activator for the tdcABCDE operon. Belongs to the LysR transcriptional regulatory family. (312 aa) |
| | garK | Glycerate kinase I; Protein involved in carbohydrate catabolic process; Belongs to the glycerate kinase type-1 family. (381 aa) |
| | garR | Tartronate semialdehyde reductase; Catalyzes the reduction of tatronate semialdehyde to D- glycerate. (294 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) |
| | agaI | Putative galactosamine-6-phosphate isomerase; Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. (251 aa) |
| | nanK | N-acetylmannosamine kinase; Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. Has also low level glucokinase activity in vitro. Belongs to the ROK (NagC/XylR) family. NanK subfamily. (291 aa) |
| | nanE | Putative N-acetylmannosamine-6-P epimerase; Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N- acetylglucosamine-6-phosphate (GlcNAc-6-P). (229 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) |
| | yheT | UPF0017 family putative hydrolase; Belongs to the AB hydrolase superfamily. AB hydrolase 4 family. (340 aa) |
| | frlA | Putative fructoselysine transporter; Is likely involved in the transport of fructoselysine and psicoselysine to the cytoplasm, where they are degraded. (445 aa) |
| | gntT | Gluconate transporter, high-affinity GNT I system; Part of the gluconate utilization system Gnt-I; high-affinity intake of gluconate. (438 aa) |
| | gntK | Gluconokinase 2, thermoresistant; gluconate transport, GNT I system; Protein involved in glucose metabolic process; Belongs to the gluconokinase GntK/GntV family. (175 aa) |
| | gntR | D-gluconate inducible gluconate regulon transcriptional repressor; Negative regulator for the gluconate utilization system GNT- I, the gntUKR operon. (331 aa) |
| | tusA | mnm(5)-s(2)U34-tRNA 2-thiolation sulfurtransferase; Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesi [...] (81 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) |
| | kdgK | 2-dehydro-3-deoxygluconokinase; 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. (309 aa) |
| | ghrB | Glyoxylate/hydroxypyruvate reductase B; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2- keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D- fructose and L-sorbose. Activity with NAD is very low; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily. (324 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) |
| | yibF | Glutathione S-transferase homolog; Glutathione (GSH) transferase homolog, that might be involved in selenium metabolism. (202 aa) |
| | tdh | L-threonine 3-dehydrogenase, NAD(P)-binding; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). Belongs to the zinc-containing alcohol dehydrogenase family. (341 aa) |
| | kbl | Glycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 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) |
| | yidR | DUF3748 family protein. (415 aa) |
| | dgoT | D-galactonate transporter; Intake of galactonate into the cell; Belongs to the major facilitator superfamily. Phthalate permease family. (430 aa) |
| | dgoK | 2-oxo-3-deoxygalactonate kinase; Protein involved in carbohydrate catabolic process; Belongs to the DgoK family. (292 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) |
| | tnaB | Tryptophan transporter of low affinity; Involved in tryptophan transport across the cytoplasmic membrane. Plays a role in transporting tryptophan which is to be used catabolically. (415 aa) |
| | yieK | Putative 6-phosphogluconolactonase; Pyrimidine-specific nucleoside hydrolase; Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. (240 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) |
| | fadA | 3-ketoacyl-CoA thiolase (thiolase I); Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. (387 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) |
| | dtd | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] (145 aa) |
| | acs | acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs 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. (652 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) |
| | 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) |
| | ulaG | L-ascorbate 6-phosphate lactonase; Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3- keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. Also shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP); Belongs to the UlaG family. (354 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) |
| | ulaE | L-xylulose 5-phosphate 3-epimerase; Catalyzes the isomerization of L-xylulose-5-phosphate to L- ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization; Belongs to the L-ribulose-5-phosphate 3-epimerase family. (284 aa) |
| | ulaF | L-ribulose 5-phosphate 4-epimerase; Catalyzes the isomerization of L-ribulose 5-phosphate to D- xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization; Belongs to the aldolase class II family. AraD/FucA subfamily. (228 aa) |
| | idnT | L-idonate and D-gluconate transporter; Transports L-idonate, D-gluconate and 5-keto-D-gluconate, from the periplasm across the inner membrane. (439 aa) |
| | idnO | 5-keto-D-gluconate-5-reductase; Catalyzes the reduction of 5-keto-D-gluconate to D-gluconate, using either NADH or NADPH. Is likely involved in an L-idonate degradation pathway that allows E.coli to utilize L-idonate as the sole carbon and energy source. Is also able to catalyze the reverse reaction in vitro, but the D-gluconate oxidation by the enzyme can only proceed with NAD; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (254 aa) |
| | idnD | L-idonate 5-dehydrogenase, NAD-binding; Catalyzes the NADH/NADPH-dependent oxidation of L-idonate to 5-ketogluconate (5KG); Belongs to the zinc-containing alcohol dehydrogenase family. (343 aa) |
| | idnK | D-gluconate kinase, thermosensitive; Protein involved in carbohydrate catabolic process; Belongs to the gluconokinase GntK/GntV family. (187 aa) |
| | yjhC | GFO/IDH/MOCA family putative oxidoreductase. NAD(P)-dependent; Putative dehydrogenase; Belongs to the Gfo/Idh/MocA family. (372 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) |
| | gntP | Fructuronate transporter; High-affinity gluconate transporter with fairly broad specificity, including low affinity for glucuronate, several disaccharides, and some hexoses, but not glucose. (447 aa) |
| | uxuA | Mannonate hydrolase; Catalyzes the dehydration of D-mannonate. (394 aa) |
| | uxuB | D-mannonate oxidoreductase, NAD-dependent; D-mannonate oxidoreductase; Protein involved in carbohydrate catabolic process; Belongs to the mannitol dehydrogenase family. UxuB subfamily. (486 aa) |
| | lgoR | Putative transcriptional activator for L-galactonate catabolism; May be a positive transcriptional regulator for lgoD and/or lgoT. Is essential for growth on L-galactonate as the sole carbon source. (304 aa) |
| | lgoD | L-galactonate oxidoreductase; Catalyzes the oxidation of L-galactonate to D-tagaturonate. Required for growth on L-galactonate as the sole carbon source. In vitro, can also use L-gulonate. (340 aa) |
| | glcF | Glycolate oxidase 4Fe-4S iron-sulfur cluster subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is required for E.coli to grow on glycolate as a sole source of carbon. Is also able to oxidize D-lactate ((R)-lactate) with a similar rate. 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. (407 aa) |
| | glcE | Glycolate oxidase FAD binding subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is required for E.coli to grow on glycolate as a sole source of carbon. Is also able to oxidize D-lactate ((R)-lactate) with a similar rate. 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. (350 aa) |
| | yhaM | Putative L-serine dehydratase alpha chain; Plays a role in L-cysteine detoxification; it has been speculated to be a cysteine desulfhydrase. (436 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) |
| | caiA | Crotonobetaine reductase subunit II, FAD-binding; Catalyzes the reduction of crotonobetainyl-CoA to gamma- butyrobetainyl-CoA. The electron donor could be the FixA/FixB complex. (380 aa) |
| | fixB | Protein FixB; Required for anaerobic carnitine reduction. May bring reductant to CaiA; Belongs to the ETF alpha-subunit/FixB family. (313 aa) |
| | nadC | Quinolinate phosphoribosyltransferase; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (297 aa) |
| | aceE | Pyruvate dehydrogenase, decarboxylase component E1, thiamine triphosphate-binding; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (887 aa) |
| | aceF | Pyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; 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). (630 aa) |
| | lpd | Dihydrolipoyl dehydrogenase; Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. (474 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) |
| | ldcC | Lysine decarboxylase 2, constitutive; Plays a role in lysine utilization by acting as a lysine decarboxylase. (713 aa) |
| | fadE | Acyl coenzyme A dehydrogenase; Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for E.coli to utilize dodecanoate or oleate as the sole carbon and energy source for growth. (814 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) |
| | 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) |
| | yahI | Carbamate kinase-like protein; Putative kinase; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the carbamate kinase family. (316 aa) |
| | prpR | Propionate catabolism operon regulatory protein; Involved in the transcriptional regulation of the propionate catabolism operon. (528 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) |
| | prpE | propionate--CoA ligase; Catalyzes the synthesis of propionyl-CoA from propionate and CoA. Also converts acetate to acetyl-CoA but with a lower specific activity (By similarity). (628 aa) |
| | mhpA | 3-(3-hydroxyphenyl)propionate hydroxylase; Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI). (554 aa) |
| | mhpB | 2,3-dihydroxyphenylpropionate 1,2-dioxygenase; Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6- ketononatrienedioate, respectively; Belongs to the LigB/MhpB extradiol dioxygenase family. (314 aa) |
| | mhpC | 2-hydroxy-6-ketonona-2,4-dienedioic acid hydrolase; Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6- oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain; Belongs to the AB hydrolase superfamily. MhpC family. (288 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) |
| | mhpF | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. (316 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) |
| | thiI | tRNA s(4)U8 sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. Belongs to the ThiI family. (482 aa) |
| | fadM | Long-chain acyl-CoA thioesterase III; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids; Belongs to the 4-hydroxybenzoyl-CoA thioesterase family. (132 aa) |
| | ybaO | Putative DNA-binding transcriptional regulator; Plays a role in L-cysteine detoxification. Binds to the dlsT(yhaO)-yhaM operon promoter in the presence but not absence of L- cysteine; activates transcription from the dlsT(yhaO)-yhaM operon. No other DNA target was identified in strain K12 / BW25113. Thiosulfate does not activate its transcription function. Overexpression doubles hydrogen sulfide production in the presence of cysteine. (152 aa) |
| | tesB | acyl-CoA thioesterase 2; Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known; Belongs to the C/M/P thioester hydrolase family. (286 aa) |
| | glsA | Putative glutaminase; Protein involved in cellular amino acid catabolic process. (310 aa) |
| | gcl | Glyoxylate carboligase; Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). (593 aa) |
| | glxR | Tartronate semialdehyde reductase, NADH-dependent; Protein involved in carbohydrate catabolic process, glycolate metabolic process and allantoin assimilation pathway; Belongs to the HIBADH-related family. (292 aa) |
| | glxK | Glycerate kinase II; Protein involved in carbohydrate catabolic process, glycolate metabolic process and allantoin assimilation pathway; Belongs to the glycerate kinase type-1 family. (381 aa) |
| | ybcF | Putative carbamate kinase; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process. (297 aa) |
| | asnB | Asparagine synthetase B; Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity. (554 aa) |
| | nagA | N-acetylglucosamine-6-phosphate deacetylase; Involved in the first step in the biosynthesis of amino- sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N- acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6- phosphate and acetate. In vitro, can also hydrolyze substrate analogs such as N-thioacetyl-D-glucosamine-6-phosphate, N-trifluoroacetyl-D- glucosamine-6-phosphate, N-acetyl-D-glucosamine-6-sulfate, N-acetyl-D- galactosamine-6-phosphate, and N-formyl-D-glucosamine-6-phosphate. (382 aa) |
| | nagB | Glucosamine-6-phosphate deaminase; Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion; Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily. (266 aa) |
| | sucB | Dihydrolipoyltranssuccinase; 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). (405 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) |
| | poxB | Pyruvate dehydrogenase, thiamine triphosphate-binding, FAD-binding; Pyruvate oxidase; Protein involved in carbohydrate catabolic process and pyruvate catabolic process; Belongs to the TPP enzyme family. (572 aa) |
| | lrp | Leucine-responsive global transcriptional regulator; Mediates a global response to leucine. Exogenous leucine affects the expression of a number of different operons; lrp mediates this effect for at least some of these operons. For example it is regulator of the branched-chain amino acid transport genes. (164 aa) |
| | pflB | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. (760 aa) |
| | putA | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon; In the C-terminal section; belongs to the aldehyde dehydrogenase family. (1320 aa) |
| | hinT | Purine nucleoside phosphoramidase, dadA activator protein; Hydrolyzes purine nucleotide phosphoramidates, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate), guanosine 5'monophosphomorpholidate (GMP-morpholidate) and tryptamine 5'guanosine monophosphate (TpGd). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine--tRNA ligase, and lysyl-GMP (GMP-N-epsilon-(N- alpha-acetyl lysine methyl ester)). Is essential for the activity of the enzyme D-alanine dehydrogenase (DadA) and is required for E [...] (119 aa) |
| | dadA | D-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. (432 aa) |
| | dadX | Alanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. (356 aa) |
| | yciA | acyl-CoA esterase; Catalyzes the hydrolysis of the thioester bond in palmitoyl- CoA and malonyl-CoA. (132 aa) |
| | puuE | 4-aminobutyrate aminotransferase, PLP-dependent; Catalyzes the transfer of the amino group from gamma- aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). PuuE is important for utilization of putrescine as the sole nitrogen or carbon source; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (421 aa) |
| | ycjG | L-Ala-D/L-Glu epimerase; Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala- L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L- Lys-L-Ala, or D-Ala-D-Ala; Belongs to the mandelate racemase/muconate lactonizing enzyme family. (321 aa) |
| | abgB | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. (481 aa) |
| | abgA | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. (436 aa) |
| | feaB | Phenylacetaldehyde dehydrogenase; Acts almost equally well on phenylacetaldehyde, 4- hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde. (499 aa) |
| | tynA | Tyramine oxidase, copper-requiring; The enzyme prefers aromatic over aliphatic amines; Belongs to the copper/topaquinone oxidase family. (757 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) |
| | paaA | Ring 1,2-phenylacetyl-CoA epoxidase subunit; Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA- CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA. (309 aa) |
| | paaB | Putative ring 1,2-phenylacetyl-CoA epoxidase subunit; Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA- CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit B may play a regulatory role or be directly involved in electron transport. (95 aa) |
| | paaC | Ring 1,2-phenylacetyl-CoA epoxidase subunit; Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA- CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit C may be essential for structural integrity of the alpha subunit. (248 aa) |
| | paaD | Ring 1,2-phenylacetyl-CoA epoxidase subunit; Possible component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit D may have a function related to the maturation of the monooxygenase complex, rather than direct involvement in catalysis. PaaD could assist either in maturation of PaaE or PaaA. (165 aa) |
| | paaE | Ring 1,2-phenylacetyl-CoA epoxidase, NAD(P)H oxidoreductase component; Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA- CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit E is a reductase with a preference for NADPH and FAD, capable of reducing cytochrome c. (356 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) |
| | 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) |
| | paaH | 3-hydroxyadipyl-CoA dehydrogenase, NAD+-dependent; Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3- oxoadipyl-CoA; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (475 aa) |
| | paaI | hydroxyphenylacetyl-CoA thioesterase; Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA. Belongs to the thioesterase PaaI family. (140 aa) |
| | paaJ | 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase; Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA. Belongs to the thiolase-like superfamily. Thiolase family. (401 aa) |
| | paaK | phenylacetyl-CoA ligase; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). (437 aa) |
| | paaX | Transcriptional repressor of phenylacetic acid degradation paa operon, phenylacetyl-CoA inducer; Negative regulator of the paaZ and paaABCDEFGHIJK catabolic operons. Binds the consensus sequence 5'-WWTRTGATTCGYGWT-3'. Binding of PaaX is specifically inhibited by phenylacetyl-coenzyme A (PA-CoA). (316 aa) |
| | paaY | Thioesterase required for phenylacetic acid degradation; trimeric; phenylacetate regulatory and detoxification protein; hexapeptide repeat protein. (196 aa) |
| | aldA | Aldehyde dehydrogenase A, NAD-linked; Acts on lactaldehyde as well as other aldehydes. (479 aa) |
| | patD | Gamma-aminobutyraldehyde dehydrogenase; Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Can also oxidize n-alkyl medium-chain aldehydes, bu [...] (474 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) |
| | uxaB | Altronate oxidoreductase, NAD-dependent; Altronate oxidoreductase; Protein involved in carbohydrate catabolic process. (483 aa) |
| | glsB | Putative glutaminase; Protein involved in cellular amino acid catabolic process. (308 aa) |
| | sad | Succinate semialdehyde dehydrogenase, NAD(P)+-dependent; Catalyzes the NAD(+)-dependent oxidation of succinate semialdehyde to succinate. It acts preferentially with NAD as cosubstrate but can also use NADP. Prevents the toxic accumulation of succinate semialdehyde (SSA) and plays an important role when arginine and putrescine are used as the sole nitrogen or carbon sources. (462 aa) |
| | rspA | Bifunctional D-altronate/D-mannonate dehydratase; Probably involved in the degradation of homoserine lactone (HSL) or of a metabolite of HSL that signals starvation. (404 aa) |
| | hdhA | 7-alpha-hydroxysteroid dehydrogenase, NAD-dependent; Catalyzes the oxidation of the 7-alpha-hydroxy group of primary bile acids such as cholate, chenodeoxycholate and taurochenodeoxycholate. To a lesser extent, also able to use taurocholate and glycocholate. (255 aa) |
| | anmK | anhydro-N-acetylmuramic acid kinase; Catalyzes the specific phosphorylation of 1,6-anhydro-N- acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling; Belongs to the anhydro-N-acetylmuramic acid kinase family. (369 aa) |
