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pabC pabC dhaM dhaM dhaL dhaL trpD trpD trpE trpE maeA maeA malY malY pykF pykF sdaA sdaA pykA pykA menD menD dsdA dsdA maeB maeB dapA dapA sdaB sdaB metC metC lldD lldD ilvB ilvB tnaA tnaA ppc ppc ubiC ubiC tdcG tdcG entB entB cof cof dxs dxs prpB prpB ilvH ilvH
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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pabC4-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)
dhaMPutative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. (472 aa)
dhaLDihydroxyacetone kinase, C-terminal domain; ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL- ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PT [...] (210 aa)
trpDAnthranilate 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)
trpEComponent 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)
maeAMalate dehydrogenase, decarboxylating, NAD-requiring; NAD-linked malate dehydrogenase (malic enzyme); Protein involved in gluconeogenesis. (565 aa)
malYPLP-dependent beta-cystathionase and maltose regulon regulator; Acts as a beta-cystathionase and as a repressor of the maltose regulon. (390 aa)
pykFPyruvate kinase I (formerly F), fructose stimulated; Protein involved in glycolysis, fermentation and anaerobic respiration. (470 aa)
sdaAL-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)
pykAPyruvate kinase II, glucose stimulated; Protein involved in glycolysis, fermentation and anaerobic respiration. (480 aa)
menD2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate synthase; Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2- succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). (556 aa)
dsdAD-serine dehydratase (deaminase); Protein involved in cellular amino acid catabolic process. (442 aa)
maeBMalic enzyme: putative oxidoreductase/phosphotransacetylase; Putative multimodular enzyme; In the N-terminal section; belongs to the malic enzymes family. (759 aa)
dapADihydrodipicolinate 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)
sdaBL-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)
metCCystathionine 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)
lldDL-lactate dehydrogenase, FMN-linked; Catalyzes the conversion of L-lactate to pyruvate. Seems to be a primary dehydrogenase in the respiratory chain. To a lesser extent, can also oxidize DL-alpha-hydroxybutyrate, but not D-lactate. (396 aa)
ilvBAcetolactate synthase I,valine-sensitive, large subunit. (562 aa)
tnaAtryptophanase/L-cysteine desulfhydrase, PLP-dependent; Tryptophanase; Protein involved in cellular amino acid catabolic process; Belongs to the beta-eliminating lyase family. (471 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. (883 aa)
ubiCChorismate pyruvate-lyase; Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. (165 aa)
tdcGL-serine dehydratase; Protein involved in cellular amino acid catabolic process. (454 aa)
entBIsochorismatase; Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. EntB is a bifunctional protein that serves as an isochorismate lyase and an aryl carrier protein (ArCP). Catalyzes the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), the precursor of 2,3- dihydroxybenzoate (DHB). In the enterob [...] (285 aa)
cofThiamine pyrimidine pyrophosphate hydrolase; Catalyzes the hydrolysis of 4-amino-2-methyl-5- hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5- hydroxymethylpyrimidine phosphate (HMP-P). Can also hydrolyze other substrates such as MeO-HMP-PP and 4-amino-2-trifluoromethyl 5- hydroxymethylpyrimidine pyrophosphate (CF3-HMP-PP) to give MeO-HMP-P and 4-amino-2-trifluoromethyl-5-hydroxymethylpyrimidine phosphate. This hydrolysis generates resistance to the antibiotics (bacimethrin, CF3- HMP) by reducing the formation of their toxic forms, 2'-methoxythiamin pyrophosphate (M [...] (272 aa)
dxs1-deoxyxylulose-5-phosphate synthase, thiamine triphosphate-binding, FAD-requiring; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP). (620 aa)
prpB2-methylisocitrate lyase; Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2- methylisocitrate to yield pyruvate and succinate via an alpha-carboxy- carbanion intermediate; Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family. (296 aa)
ilvHAcetolactate synthase III, valine sensitive, small subunit. (163 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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