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ppsA ppsA shiA shiA glf glf ldhA ldhA feaB feaB tynA tynA paaI paaI fumC fumC ydiB ydiB astC astC trpR trpR yjiC yjiC frdB frdB tyrB tyrB birA birA tnaA tnaA aroB aroB pabA pabA accB accB galP galP tktA tktA tyrA tyrA pheA pheA entD entD entC entC entB entB entA entA gltA gltA sucC sucC aroG aroG ybiC ybiC pflB pflB pabC pabC ptsG ptsG icd icd adhE adhE trpC trpC trpD trpD trpE trpE tyrR tyrR
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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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a 3D structure is known or predicted
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ppsAPhosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. (792 aa)
shiAShikimate transporter; Pseudogene, glycosyltransferase homology. (438 aa)
glfUDP-galactopyranose mutase, FAD/NAD(P)-binding; Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF); Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase family. (367 aa)
ldhAFermentative D-lactate dehydrogenase, NAD-dependent; Fermentative lactate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (329 aa)
feaBPhenylacetaldehyde dehydrogenase; Acts almost equally well on phenylacetaldehyde, 4- hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde. (499 aa)
tynATyramine oxidase, copper-requiring; The enzyme prefers aromatic over aliphatic amines; Belongs to the copper/topaquinone oxidase family. (757 aa)
paaIhydroxyphenylacetyl-CoA thioesterase; Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA. Belongs to the thioesterase PaaI family. (140 aa)
fumCFumarate hydratase (fumarase C),aerobic Class II; Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress. Catalyzes the stereospecific interconversion of fumarate to L-malate. Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (467 aa)
ydiBQuinate/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)
astCSuccinylornithine 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)
trpRTranscriptional repressor, tryptophan-binding; This protein is an aporepressor. When complexed with L- tryptophan it binds the operator region of the trp operon (5'- ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. (108 aa)
yjiCUncharacterized protein; To E.coli YjfZ. (276 aa)
frdBFumarate reductase (anaerobic), Fe-S subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (244 aa)
tyrBTyrosine 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)
birABifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. (321 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)
aroB3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). (362 aa)
pabAAminodeoxychorismate 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)
accBBiotin carboxyl carrier protein of acetyl-CoA carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (156 aa)
galPD-galactose transporter; Uptake of galactose across the boundary membrane with the concomitant transport of protons into the cell (symport system); Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. (464 aa)
tktATransketolase 1, thiamine triphosphate-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. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose- 5-phosphate. (663 aa)
tyrAChorismate mutase-T and prephenate dehydrogenase; Protein involved in L-phenylalanine biosynthetic process and tyrosine biosynthetic process. (373 aa)
pheAChorismate mutase and prephenate dehydratase, P-protein; Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. (386 aa)
entDPhosphopantetheinyltransferase component of enterobactin synthase multienzyme complex; 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. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP do [...] (206 aa)
entCIsochorismate synthase 1; Involved in the biosynthesis of the siderophore enterobactin (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate. (391 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)
entA2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. Catalyzes the reversible NAD-dependent oxidation of the C3-hydroxyl group of 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), producing the transient intermediate 2-hydroxy-3-oxo-4,6- cyclohexadiene-1-carboxylate, which undergoes rapid aromatization to the final product, 2,3-dihydroxybenzoate (2,3-DHB). Only the compounds with a C3-hydroxyl group such as methyl 2,3-dihydro-2,3- dihydroxyb [...] (248 aa)
gltACitrate synthase; Protein involved in tricarboxylic acid cycle and anaerobic respiration; Belongs to the citrate synthase family. (427 aa)
sucCsuccinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly impor [...] (388 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); Belongs to the class-I DAHP synthase family. (350 aa)
ybiCPutative dehydrogenase; Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. (361 aa)
pflBFormate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. (760 aa)
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)
ptsGFused glucose-specific PTS enzymes: IIB component/IIC component; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport. Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration and an effector modulating the activity of the transcriptional repressor Mlc. (477 aa)
icdIsocitrate dehydrogenase, specific for NADP+; Protein involved in tricarboxylic acid cycle and anaerobic respiration; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (416 aa)
adhEAcetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. (891 aa)
trpCIndole-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)
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)
tyrRAromatic amino acid biosynthesis and transport regulon transcriptional regulator; Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP ge [...] (513 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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