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thrA thrA thrB thrB thrC thrC talB talB dapB dapB leuD leuD leuC leuC leuB leuB leuA leuA ilvI ilvI ilvH ilvH acnB acnB pfs pfs dapD dapD aroL aroL proC proC proA proA proB proB asnB asnB gltA gltA aroG aroG gpmA gpmA ybhJ ybhJ ltaE ltaE fbaB fbaB hisI hisI hisF hisF hisA hisA hisH hisH hisB hisB hisC hisC hisD hisD hisG hisG pykA pykA sdaA sdaA gapA gapA pfkB pfkB aroH aroH aroD aroD pykF pykF malY malY prsA prsA trpA trpA trpB trpB trpC trpC trpD trpD trpE trpE acnA acnA icd-2 icd-2 aspC aspC aroA aroA serC serC yfbQ yfbQ aroC aroC cysK cysK cysM cysM talA talA tktB tktB dapE dapE dapA dapA glyA glyA pheA pheA tyrA tyrA aroF aroF luxS luxS dapF dapF ilvC ilvC ilvA ilvA ilvD ilvD ilvE ilvE ilvM ilvM ilvG ilvG argH argH argB argB argC argC argE argE metL metL metB metB tpiA tpiA pfkA pfkA glnA glnA metE metE eno eno sdaB sdaB argA argA lysA lysA serA serA rpiA rpiA fbaA fbaA pgk pgk tktA tktA metK metK metC metC tdcG tdcG tdcB tdcB argG argG gltB gltB gltD gltD aroE aroE argD argD rpe rpe aroB aroB aroK aroK asd asd cysE cysE gpmI gpmI CAR20287.1 CAR20287.1 CAR20288.1 CAR20288.1 CAR20303.1 CAR20303.1 ilvN ilvN ilvB ilvB asnA asnA metA metA metH metH CAR20517.1 CAR20517.1 lysC lysC tyrB tyrB rpiB rpiB arcB-2 arcB-2 argI argI serB serB ytjC ytjC
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thrAFused aspartokinase I; Function experimentally demonstrated in the studied species; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. (820 aa)
thrBHomoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (310 aa)
thrCThreonine synthase; Function experimentally demonstrated in the studied species; enzyme. (428 aa)
talBTransaldolase B; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (317 aa)
dapBDihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. (273 aa)
leuD3-isopropylmalate isomerase subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (201 aa)
leuC3-isopropylmalate isomerase subunit, dehydratase component; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (466 aa)
leuB3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. (363 aa)
leuA2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (523 aa)
ilvIAcetolactate synthase III, large subunit; Function experimentally demonstrated in the studied species; enzyme. (574 aa)
ilvHAcetolactate synthase III, thiamin-dependent, small subunit; Function experimentally demonstrated in the studied species; enzyme. (163 aa)
acnBBifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aconitase/IPM isomerase family. (865 aa)
pfs5'-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 accumulatio [...] (232 aa)
dapD2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Function experimentally demonstrated in the studied species; enzyme. (274 aa)
aroLShikimate kinase II; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. (174 aa)
proCPyrroline-5-carboxylate reductase, NAD(P)-binding; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (269 aa)
proAGamma-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)
proBGamma-glutamate kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (367 aa)
asnBAsparagine synthetase B; Function experimentally demonstrated in the studied species; enzyme. (554 aa)
gltACitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (427 aa)
aroG3-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). (350 aa)
gpmAPhosphoglyceromutase 1; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily. (250 aa)
ybhJPutative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (674 aa)
ltaEL-allo-threonine aldolase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (333 aa)
fbaBFructose-bisphosphate aldolase class I; Function experimentally demonstrated in the studied species; enzyme. (350 aa)
hisIFused phosphoribosyl-AMP cyclohydrolase; Function experimentally demonstrated in the studied species; enzyme; In the N-terminal section; belongs to the PRA-CH family. (203 aa)
hisFImidazole 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. (258 aa)
hisAN-(5'-phospho-L-ribosyl-formimino)-5-amino-1- (5'-phosphoribosyl)-4-imidazolecarboxamide isomerase; Function experimentally demonstrated in the studied species; enzyme. (245 aa)
hisHImidazole glycerol phosphate synthase, glutamine amidotransferase subunit with HisF; 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)
hisBFused histidinol-phosphatase; Function experimentally demonstrated in the studied species; enzyme; In the N-terminal section; belongs to the histidinol- phosphatase family. (355 aa)
hisCHistidinol-phosphate aminotransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (356 aa)
hisDBifunctional histidinal dehydrogenase and histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (434 aa)
hisGATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. (299 aa)
pykAPyruvate kinase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (480 aa)
sdaAL-serine deaminase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
gapAGlyceraldehyde-3-phosphate dehydrogenase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. (331 aa)
pfkB6-phosphofructokinase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the carbohydrate kinase PfkB family. (309 aa)
aroH3-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)
aroD3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. Belongs to the type-I 3-dehydroquinase family. (252 aa)
pykFPyruvate kinase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (470 aa)
malYBifunctional beta-cystathionase, PLP-dependent and regulator of maltose regulon; Function experimentally demonstrated in the studied species; enzyme. (390 aa)
prsAPhosphoribosylpyrophosphate synthase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily. (315 aa)
trpATryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (268 aa)
trpBTryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (397 aa)
trpCFused indole-3-glycerolphosphate synthetase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the TrpC family. (452 aa)
trpDFused glutamine amidotransferase (component II) of anthranilate synthase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (531 aa)
trpEComponent I of anthranilate synthase; Function experimentally demonstrated in the studied species; enzyme. (520 aa)
acnAAconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (891 aa)
icd-2Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. (416 aa)
aspCAspartate aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (396 aa)
aroA5-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)
serC3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (362 aa)
yfbQPutative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (405 aa)
aroCChorismate 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. (361 aa)
cysKCysteine synthase A, O-acetylserine sulfhydrolase A subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the cysteine synthase/cystathionine beta- synthase family. (323 aa)
cysMCysteine synthase B (O-acetylserine sulfhydrolase B); Function experimentally demonstrated in the studied species; enzyme; Belongs to the cysteine synthase/cystathionine beta- synthase family. (303 aa)
talATransaldolase A; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (316 aa)
tktBTransketolase 2, thiamin-binding; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. (667 aa)
dapEN-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)
dapADihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (292 aa)
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (417 aa)
pheAFused chorismate mutase P; Function experimentally demonstrated in the studied species; enzyme. (386 aa)
tyrAFused chorismate mutase T; Function experimentally demonstrated in the studied species; enzyme. (373 aa)
aroF3-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). (356 aa)
luxSS-ribosylhomocysteinase; 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)
dapFDiaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. (274 aa)
ilvCKetol-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. (491 aa)
ilvAThreonine deaminase; 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)
ilvDDihydroxyacid dehydratase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the IlvD/Edd family. (616 aa)
ilvEBranched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (309 aa)
ilvMAcetolactate synthase II, small subunit; Function experimentally demonstrated in the studied species; enzyme. (87 aa)
ilvGAcetolactate synthase; Function of strongly homologous gene; enzyme. (548 aa)
argHArgininosuccinate lyase; Function experimentally demonstrated in the studied species; enzyme. (457 aa)
argBAcetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate. (257 aa)
argCN-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)
argEAcetylornithine deacetylase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the peptidase M20A family. ArgE subfamily. (383 aa)
metLFused aspartokinase II; Function experimentally demonstrated in the studied species; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. (810 aa)
metBCystathionine gamma-synthase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (386 aa)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
pfkA6-phosphofructokinase I; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. (320 aa)
glnAGlutamine synthetase; Function experimentally demonstrated in the studied species; enzyme. (469 aa)
metE5-methyltetrahydropteroyltriglutamate- homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family. (753 aa)
enoEnolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. (432 aa)
sdaBL-serine deaminase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (455 aa)
argAFused acetylglutamate kinase homolog (inactive); Function experimentally demonstrated in the studied species; enzyme; Belongs to the acetyltransferase family. ArgA subfamily. (443 aa)
lysADiaminopimelate decarboxylase, PLP-binding; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (420 aa)
serAD-3-phosphoglycerate dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (410 aa)
rpiARibose 5-phosphate isomerase, constitutive; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. (219 aa)
fbaAFructose-bisphosphate aldolase, class II; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis; Belongs to the class II fructose-bisphosphate aldolase family. (359 aa)
pgkPhosphoglycerate kinase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the phosphoglycerate kinase family. (387 aa)
tktATransketolase 1, thiamin-binding; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. (663 aa)
metKMethionine adenosyltransferase 1; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (384 aa)
metCCystathionine beta-lyase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (395 aa)
tdcGL-serine dehydratase 3; Function experimentally demonstrated in the studied species; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
tdcBCatabolic threonine dehydratase, PLP-dependent; 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. (329 aa)
argGArgininosuccinate synthetase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the argininosuccinate synthase family. Type 2 subfamily. (447 aa)
gltBGlutamate synthase, large subunit; Function experimentally demonstrated in the studied species; enzyme. (1517 aa)
gltDGlutamate synthase, 4Fe-4S protein, small subunit; Function experimentally demonstrated in the studied species; carrier. (472 aa)
aroEDehydroshikimate 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). (272 aa)
argDBifunctional 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. (407 aa)
rpeD-ribulose-5-phosphate 3-epimerase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the ribulose-phosphate 3-epimerase family. (225 aa)
aroB3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ); Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family. (362 aa)
aroKShikimate 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)
asdAspartate-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; Belongs to the aspartate-semialdehyde dehydrogenase family. (367 aa)
cysESerine acetyltransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the transferase hexapeptide repeat family. (273 aa)
gpmIPhosphoglycero mutase III, cofactor-independent; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (514 aa)
CAR20287.1Putative fructose-bisphosphate aldolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (286 aa)
CAR20288.1Putative sugar aldolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (283 aa)
CAR20303.1Putative Aspartate transaminase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (430 aa)
ilvNAcetolactate synthase I, small subunit; Function experimentally demonstrated in the studied species; enzyme. (96 aa)
ilvBAcetolactate synthase I, large subunit; Function experimentally demonstrated in the studied species; enzyme. (562 aa)
asnAAsparagine synthetase A; Function experimentally demonstrated in the studied species; enzyme. (330 aa)
metAHomoserine transsuccinylase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. (309 aa)
metHhomocysteine-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)
CAR20517.1Putative Shikimate dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (270 aa)
lysCAspartokinase III; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aspartokinase family. (449 aa)
tyrBTyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (397 aa)
rpiBRibose 5-phosphate isomerase B/allose 6-phosphate isomerase; Function experimentally demonstrated in the studied species; enzyme. (149 aa)
arcB-2Ornithine carbamoyltransferase, catabolic (OTCase); Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family. (343 aa)
argIOrnithine 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; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family. (334 aa)
serB3-phosphoserine phosphatase; Function experimentally demonstrated in the studied species; enzyme. (322 aa)
ytjCPhosphoglyceromutase 2, co-factor independent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the phosphoglycerate mutase family. GpmB subfamily. (215 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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