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| | ilvC | Ketol-acid reductoisomerase, NAD(P)-binding; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate [...] (491 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) |
| | ilvD | Dihydroxyacid dehydratase. (616 aa) |
| | ilvE | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. (309 aa) |
| | ilvM | Pseudogene, acetolactate synthase 2 large subunit, valine-insensitive; acetolactate synthase II, large subunit, cryptic, interrupted. (87 aa) |
| | ilvL | ilvGEDA operon leader peptide. (32 aa) |
| | asnA | Asparagine synthetase A; May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn. (330 aa) |
| | glmS | L-glutamine:D-fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (609 aa) |
| | yieE | Phosphopantetheinyl transferase superfamily protein. (249 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) |
| | 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) |
| | ivbL | ilvB operon leader peptide; This protein is involved in control of the biosynthesis of isoleucine, leucine, and valine. (32 aa) |
| | ilvB | Acetolactate synthase I,valine-sensitive, large subunit. (562 aa) |
| | ilvN | Acetolactate synthase I, valine sensitive, small subunit. (96 aa) |
| | kbl | Glycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 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) |
| | cysE | Serine acetyltransferase; Protein involved in cysteine biosynthetic process; Belongs to the transferase hexapeptide repeat family. (273 aa) |
| | yibF | Glutathione S-transferase homolog; Glutathione (GSH) transferase homolog, that might be involved in selenium metabolism. (202 aa) |
| | selA | Selenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Requires selenophosphate as the selenium-donor molecule; Belongs to the SelA family. (463 aa) |
| | selB | selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily. (614 aa) |
| | avtA | Valine-pyruvate aminotransferase; Involved in the biosynthesis of alanine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (417 aa) |
| | glyQ | Glycine tRNA synthetase, alpha subunit; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-II aminoacyl-tRNA synthetase family. (303 aa) |
| | glyS | Glycine tRNA synthetase, beta subunit; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-II aminoacyl-tRNA synthetase family. (689 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) |
| | acpT | 4'-phosphopantetheinyl transferase; May be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis in E.coli. The native apo-protein substrate is unknown. Is able to functionally replace AcpS in vivo but only when expressed at high levels. Belongs to the P-Pant transferase superfamily. Gsp/Sfp/HetI/AcpT family. (195 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) |
| | ggt | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] (580 aa) |
| | asd | Aspartate-semialdehyde dehydrogenase, NAD(P)-binding; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate. (367 aa) |
| | aroK | Shikimate kinase I; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. Belongs to the shikimate kinase family. (173 aa) |
| | thrL | Thr operon leader peptide; This protein is involved in control of the biosynthesis of threonine. (21 aa) |
| | thrA | Bifunctional: aspartokinase I (N-terminal); homoserine dehydrogenase I (C-terminal); Protein involved in threonine biosynthetic process, methionine biosynthetic process and homoserine biosynthetic process. (820 aa) |
| | thrB | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. Is also able to phosphorylate the hydroxy group on gamma-carbon of L-homoserine analogs when the functional group at the alpha-position is a carboxyl, an ester, or even a hydroxymethyl group. Neither L-threonine nor L-serine are substrates of the enzyme. (310 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) |
| | ileS | isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). (938 aa) |
| | dapB | Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH. Belongs to the DapB family. (273 aa) |
| | carA | Carbamoyl phosphate synthetase small subunit, glutamine amidotransferase; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process. (382 aa) |
| | carB | Carbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family. (1073 aa) |
| | folA | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. (159 aa) |
| | leuD | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (201 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) |
| | leuB | 3-isopropylmalate dehydrogenase, NAD(+)-dependent; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. (363 aa) |
| | leuA | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (523 aa) |
| | leuL | Leu operon leader peptide; Involved in control of the biosynthesis of leucine. (28 aa) |
| | ilvI | Acetolactate synthase III, valine sensitive, large subunit. (574 aa) |
| | ilvH | Acetolactate synthase III, valine sensitive, small subunit. (163 aa) |
| | nadC | Quinolinate phosphoribosyltransferase; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (297 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) |
| | panD | Aspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine; Belongs to the PanD family. (126 aa) |
| | gluQ | glutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis. (308 aa) |
| | mtn | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5- deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulati [...] (232 aa) |
| | dapD | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Protein involved in lysine biosynthetic process via diaminopimelate; Belongs to the transferase hexapeptide repeat family. (274 aa) |
| | ldcC | Lysine decarboxylase 2, constitutive; Plays a role in lysine utilization by acting as a lysine decarboxylase. (713 aa) |
| | proS | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] (572 aa) |
| | yafJ | Type 2 glutamine amidotransferase family protein; Putative amidotransferase. (255 aa) |
| | proB | Gamma-glutamate kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (367 aa) |
| | proA | Gamma-glutamylphosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. (417 aa) |
| | mmuP | CP4-6 prophage; Transporter for the intake of S-methylmethionine; Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family. (467 aa) |
| | mmuM | CP4-6 prophage; Catalyzes methyl transfer from S-methylmethionine or S- adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine. (310 aa) |
| | argF | Ornithine carbamoyltransferase 2, chain F; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. (334 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) |
| | 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) |
| | proC | Pyrroline-5-carboxylate reductase, NAD(P)-binding; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. Does not catalyze the reverse reaction. (269 aa) |
| | aroL | Shikimate kinase II; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. Belongs to the shikimate kinase family. AroL subfamily. (174 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) |
| | 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) |
| | 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) |
| | ybcF | Putative carbamate kinase; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process. (297 aa) |
| | cysS | Cysteine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa) |
| | folD | Methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP. (288 aa) |
| | entF | Enterobactin synthase multienzyme complex component, ATP-dependent; Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE). (1293 aa) |
| | ybdL | Methionine aminotransferase, PLP-dependent; Shows aminotransferase activity with methionine and histidine as substrates, and to a lesser extent also with phenylalanine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (386 aa) |
| | nadD | Nicotinic acid mononucleotide adenylyltransferase, NAD(P)-dependent; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). Belongs to the NadD family. (213 aa) |
| | leuS | Leucine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 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) |
| | glnS | Glutamine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (554 aa) |
| | speF | Ornithine decarboxylase isozyme, inducible; Protein involved in polyamine biosynthetic process; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (732 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) |
| | nadA | Quinolinate synthase, subunit A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. Belongs to the quinolinate synthase A family. Type 1 subfamily. (347 aa) |
| | aroG | 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, phenylalanine repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP); Belongs to the class-I DAHP synthase family. (350 aa) |
| | ybiB | Putative family 3 glycosyltransferase; Putative enzyme; Belongs to the anthranilate phosphoribosyltransferase family. (320 aa) |
| | grxA | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. (85 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) |
| | 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) |
| | serS | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (430 aa) |
| | pflB | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. (760 aa) |
| | serC | 3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both pyridoxine and serine biosynthesis; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (362 aa) |
| | aroA | 5-enolpyruvylshikimate-3-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. (427 aa) |
| | aspC | Aspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. (396 aa) |
| | asnS | Asparagine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (466 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) |
| | 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) |
| | 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) |
| | hemA | Glutamyl tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. (418 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) |
| | 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) |
| | 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) |
| | 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) |
| | 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) |
| | trpL | Trp operon leader peptide; This protein is involved in control of the biosynthesis of tryptophan. (14 aa) |
| | cysB | N-acetylserine-responsive cysteine regulon transcriptional activator; This protein is a positive regulator of gene expression for the cysteine regulon, a system of 10 or more loci involved in the biosynthesis of L-cysteine from inorganic sulfate. The inducer for CysB is N-acetylserine. CysB inhibits its own transcription. (324 aa) |
| | puuA | Glutamate--putrescine ligase; Involved in the breakdown of putrescine via the biosynthesis of gamma-L-glutamylputrescine. It is able to use several diamines, spermidine and spermine. Absolutely essential to utilize putrescine as both nitrogen and carbon sources and to decrease the toxicity of putrescine, which can lead to inhibition of cell growth and protein synthesis; Belongs to the glutamine synthetase family. (472 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) |
| | 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) |
| | aldA | Aldehyde dehydrogenase A, NAD-linked; Acts on lactaldehyde as well as other aldehydes. (479 aa) |
| | ydcR | Multi modular; putative transcriptional regulator; also putative ATP-binding component of a transport system; Protein involved in ATP-binding cassette (ABC) transporter activity and regulation of transcription, DNA-dependent; In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (468 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) |
| | 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) |
| | malY | PLP-dependent beta-cystathionase and maltose regulon regulator; Acts as a beta-cystathionase and as a repressor of the maltose regulon. (390 aa) |
| | tyrS | tyrosyl-tRNA synthetase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine. (424 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) |
| | ydiB | Quinate/shikimate 5-dehydrogenase, NAD(P)-binding; The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. (288 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) |
| | aroH | 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, tryptophan repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (348 aa) |
| | pheT | Phenylalanine tRNA synthetase, beta-subunit; Protein involved in tRNA aminoacylation for protein translation. (795 aa) |
| | pheS | Phenylalanine tRNA synthetase, alpha-subunit; Protein involved in tRNA aminoacylation for protein translation. (327 aa) |
| | thrS | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] (642 aa) |
| | nadE | NAD synthetase, NH3/glutamine-dependent; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (275 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) |
| | ynjE | Molybdopterin synthase sulfurtransferase; Putative thiosulfate sulfur transferase; Protein involved in sulfur metabolic process. (435 aa) |
| | gdhA | Glutamate dehydrogenase, NADP-specific; Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. (447 aa) |
| | selD | Selenophosphate synthase; Synthesizes selenophosphate from selenide and ATP; Belongs to the selenophosphate synthase 1 family. Class I subfamily. (347 aa) |
| | ansA | Cytoplasmic L-asparaginase 1; Protein involved in cellular amino acid catabolic process; Belongs to the asparaginase 1 family. (338 aa) |
| | pabB | Aminodeoxychorismate synthase, subunit I; Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabB, in the absence of PabA, can catalyze the formation of ADC in the presence of exogenous ammonia. (453 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) |
| | aspS | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Also mischarges tRNA(Asp) with D-aspartate, although it is a poor substrate ; Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (590 aa) |
| | argS | Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (577 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) |
| | cbl | ssuEADCB/tauABCD operon transcriptional activator; May be an accessory regulatory protein within the cys regulon. (316 aa) |
| | hisL | His operon leader peptide; Protein involved in histidine biosynthetic process. (16 aa) |
| | hisG | ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. (299 aa) |
| | hisD | Bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (434 aa) |
| | hisC | Histidinol-phosphate aminotransferase; Protein involved in histidine biosynthetic process; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (356 aa) |
| | hisB | Imidazoleglycerolphosphate dehydratase and histidinol-phosphate phosphatase; Protein involved in histidine biosynthetic process. (355 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) |
| | hisA | N-(5'-phospho-L-ribosyl-formimino)-5-amino-1- (5'-phosphoribosyl)-4-imidazolecarboxamide isomerase; Protein involved in histidine biosynthetic process; Belongs to the HisA/HisF family. (245 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) |
| | hisI | Phosphoribosyl-amp cyclohydrolase; phosphoribosyl-ATP pyrophosphatase; Protein involved in histidine biosynthetic process; In the C-terminal section; belongs to the PRA-PH family. (203 aa) |
| | wcaB | Putative transferase; Protein involved in colanic acid biosynthetic process. (162 aa) |
| | metG | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. (677 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) |
| | alaA | Glutamate-pyruvate aminotransferase; Involved in the biosynthesis of alanine. (405 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) |
| | purF | Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. Can also use NH(3) in place of glutamine. (505 aa) |
| | usg | Putative semialdehyde dehydrogenase; Putative PTS system enzyme II A component. (337 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) |
| | dsdA | D-serine dehydratase (deaminase); Protein involved in cellular amino acid catabolic process. (442 aa) |
| | alaC | Glutamate-pyruvate aminotransferase; Involved in the biosynthesis of alanine. (412 aa) |
| | gltX | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (471 aa) |
| | cysZ | Sulfate transporter, sulfite inhibited; High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway. Does not transport thiosulfate. Belongs to the CysZ family. (253 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) |
| | 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) |
| | 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) |
| | eutB | Ethanolamine ammonia-lyase, heavy chain; Protein involved in amine catabolic process. (453 aa) |
| | dapE | N-succinyl-diaminopimelate deacylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. (375 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) |
| | guaA | GMP synthetase (glutamine aminotransferase); Catalyzes the synthesis of GMP from XMP. (525 aa) |
| | hisS | Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (424 aa) |
| | sseA | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. (281 aa) |
| | 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) |
| | 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) |
| | 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) |
| | purL | Phosphoribosylformyl-glycineamide synthetase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. (1295 aa) |
| | nadB | Quinolinate synthase, L-aspartate oxidase (B protein) subunit; Catalyzes the oxidation of L-aspartate to iminoaspartate. (540 aa) |
| | grcA | Autonomous glycyl radical cofactor; Acts as a radical domain for damaged PFL and possibly other radical proteins. (127 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) |
| | tyrA | Chorismate mutase-T and prephenate dehydrogenase; Protein involved in L-phenylalanine biosynthetic process and tyrosine biosynthetic process. (373 aa) |
| | aroF | 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, tyrosine-repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP); Belongs to the class-I DAHP synthase family. (356 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) |
| | 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) |
| | alaS | alanyl-tRNA synthetase; Catalyzes the attachment of L-alanine to tRNA(Ala) in a two- step reaction: L-alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller amino acid glycine as well as the sterically larger amino acid L-serine; generates 2-fold more mischarged Gly than Ser. These mischarged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Ala, Gly and Ser) in the charging step. Attaches Ala to transfer-me [...] (876 aa) |
| | cysI | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (570 aa) |
| | cysJ | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. (599 aa) |
| | pyrG | CTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (545 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) |
| | argA | Amino acid N-acetyltransferase and inactive acetylglutamate kinase; N-acetylglutamate synthase; amino acid acetyltransferase; Protein involved in arginine biosynthetic process; Belongs to the acetyltransferase family. ArgA subfamily. (443 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) |
| | lysR | Transcriptional activator of lysA; This protein activates the transcription of the lysA gene encoding diaminopimelate decarboxylase. LysR is also a negative regulator of its own expression; Belongs to the LysR transcriptional regulatory family. (311 aa) |
| | ygeW | Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. (396 aa) |
| | yqeA | Putative kinase; Belongs to the carbamate kinase family. (310 aa) |
| | ygfK | Putative Fe-S subunit oxidoreductase subunit; Could be an iron-sulfur flavoprotein with NADPH:O(2) oxidoreductase activity. (1032 aa) |
| | lysS | Lysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 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) |
| | serA | D-3-phosphoglycerate dehydrogenase; Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. (410 aa) |
| | speB | Agmatinase; Catalyzes the formation of putrescine from agmatine. (306 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) |
| | 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) |
| | 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) |
| | 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) |
| | argG | Argininosuccinate synthetase; Protein involved in arginine biosynthetic process; Belongs to the argininosuccinate synthase family. Type 2 subfamily. (447 aa) |
| | rpoN | RNA polymerase, sigma 54 (sigma N) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of enzymes involved in arginine catabolism. The open complex (sigma-54 and core RNA polymerase) serves as the receptor for the receipt of the melting signal from the remotely bound activator protein GlnG(NtrC). (477 aa) |
| | gltB | Glutamate synthase, large subunit; Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. (1486 aa) |
| | gltD | Glutamate synthase, 4Fe-4S protein, small subunit; Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. (472 aa) |
| | argR | L-arginine-responsive arginine metabolism regulon transcriptional regulator; Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1; Belongs to the ArgR family. (156 aa) |
| | aroE | Dehydroshikimate reductase, NAD(P)-binding; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It displays no activity in the presence of NAD. (272 aa) |
| | argD | Bifunctional acetylornithine aminotransferase and succinyldiaminopimelate aminotransferase; Involved in both the arginine and lysine biosynthetic pathways; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (406 aa) |
| | pabA | Aminodeoxychorismate synthase, subunit II; Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. (187 aa) |
| | frlA | Putative fructoselysine transporter; Is likely involved in the transport of fructoselysine and psicoselysine to the cytoplasm, where they are degraded. (445 aa) |
| | trpS | tryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Amino acylates tRNA(Trp) with both L- and D-tryptophan, although D-tryptophan is a poor substrate ; Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa) |
| | aroB | 3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). (362 aa) |
| | dgoD | D-galactonate dehydratase; Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy- D-galactonate. (382 aa) |
| | tdcG | L-serine dehydratase; Protein involved in cellular amino acid catabolic process. (454 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) |
| | serB | 3-phosphoserine phosphatase; Catalyzes the dephosphorylation of phosphoserine (P-Ser). Also catalyzes the hydrolysis of phosphothreonine (P-Thr). Belongs to the HAD-like hydrolase superfamily. SerB family. (322 aa) |
| | yjiR | Uncharacterized HTH-type transcriptional regulator YjiR; RIP347 (repetitive extragenic palindromic) element; contains 2 REP sequences and 1 IHF site; In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (470 aa) |
| | valS | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner. (951 aa) |
| | argI | Ornithine carbamoyltransferase 1; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. (334 aa) |
| | pyrB | Aspartate carbamoyltransferase, catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. (311 aa) |
| | ridA | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. (128 aa) |
| | epmA | Elongation Factor P Lys34 lysyltransferase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta- lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF- P 'Lys-34'. The substrate (R)-beta-lysine is 100-fold more efficient than either (S)-beta-lysine or L-alpha-lysine. Cannot ligate lysine to any tRNA. (325 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) |
| | 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) |
| | lysU | Lysine tRNA synthetase, inducible; Also can synthesize a number of adenyl dinucleotides (in particular AppppA). These dinucleotides have been proposed to act as modulators of the heat-shock response and stress response; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 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) |
| | tyrB | Tyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (397 aa) |
| | alr | Alanine racemase, biosynthetic, PLP-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. (359 aa) |
| | lysC | Lysine-sensitive aspartokinase 3; Aspartokinase III, lysine sensitive; Protein involved in lysine biosynthetic process via diaminopimelate and homoserine biosynthetic process. (449 aa) |
| | metH | homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. (1227 aa) |
| | metA | Homoserine O-transsuccinylase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the succinyl group of succinyl-CoA is initially transferred to the enzyme to form a succinyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O- succinylhomoserine. Cannot use acetyl-CoA. Belongs to the MetA family. (309 aa) |
| | hemE | Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (354 aa) |
| | argH | Argininosuccinate lyase; Protein involved in arginine biosynthetic process. (457 aa) |
| | argB | Acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. (258 aa) |
| | argC | N-acetyl-gamma-glutamylphosphate reductase, NAD(P)-binding; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. (334 aa) |
| | argE | Acetylornithine deacetylase; Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde. (383 aa) |
| | metF | 5,10-methylenetetrahydrofolate reductase; Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine. (296 aa) |
| | metL | Bifunctional aspartokinase/homoserine dehydrogenase 2; Aspartokinase II and homoserine dehydrogenase II; Protein involved in methionine biosynthetic process and homoserine biosynthetic process. (810 aa) |
| | metB | Cystathionine gamma-synthase, PLP-dependent; Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia. (386 aa) |
| | metJ | Transcriptional repressor, S-adenosylmethionine-binding; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated. (105 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) |
| | glnA | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. (469 aa) |
| | metE | 5-methyltetrahydropteroyltriglutamate- homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation. (753 aa) |
| | metR | Methionine biosynthesis regulon transcriptional regulator; Control of the last step in methionine biosynthesis; MetR is a positive activator of the metA, metE and metH genes. MetR is also a negative regulator of its own expression. Binds homocysteine as an inducer; Belongs to the LysR transcriptional regulatory family. (317 aa) |
| | dapF | Diaminopimelate epimerase; Involved in the succinylase branch of the L-lysine biosynthesis and in the biosynthesis of the pentapeptide incorporated in the peptidoglycan moiety. Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso- diaminoheptanedioate (meso-DAP). (274 aa) |
| | ilvY | Transcriptional activator of ilvC; This protein activates the transcription of the ilvC gene in the presence of acetolactate or acetohydroxybutyrate. IlvY is also a negative regulator of its own expression; Belongs to the LysR transcriptional regulatory family. (297 aa) |
