STRINGSTRING
fbp fbp thrA thrA thrB thrB talB talB pdxA pdxA ilvH ilvH gmhB gmhB dxs dxs ybhA ybhA pgl pgl ltaE ltaE serC serC pykF pykF ppsA ppsA gapA gapA nudL nudL pykA pykA hisB hisB pdxB pdxB talA talA tktB tktB rpoS rpoS tktA tktA rng rng php php gph gph aroB aroB ilvE ilvE ilvA ilvA yigL yigL tpiA tpiA metL metL rpoC rpoC pgi pgi tyrB tyrB yjbQ yjbQ nadR nadR
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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fbpProtein involved in gluconeogenesis. (332 aa)
thrABifunctional: aspartokinase I (N-terminal); homoserine dehydrogenase I (C-terminal); Protein involved in threonine biosynthetic process, methionine biosynthetic process and homoserine biosynthetic process. (820 aa)
thrBHomoserine 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)
talBTransaldolase B; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (317 aa)
pdxA4-hydroxy-L-threonine phosphate dehydrogenase, NAD-dependent; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP); Belongs to the PdxA family. (329 aa)
ilvHAcetolactate synthase III, valine sensitive, small subunit. (163 aa)
gmhBD,D-heptose 1,7-bisphosphate phosphatase; Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position. (191 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)
ybhAPyridoxal phosphate (PLP) phosphatase; Catalyzes the dephosphorylation of pyridoxal-phosphate (PLP). Can also hydrolyze erythrose-4-phosphate (Ery4P) and fructose-1,6-bis- phosphate (Fru1,6bisP); Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. (272 aa)
pgl6-phosphogluconolactonase; Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. (331 aa)
ltaEL-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)
serC3-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)
pykFPyruvate kinase I (formerly F), fructose stimulated; Protein involved in glycolysis, fermentation and anaerobic respiration. (470 aa)
ppsAPhosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. (792 aa)
gapAGlyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. (331 aa)
nudLPutative CoA pyrophosphohydrolase, weak 3-phosphohydroxypyruvate phosphatase; Probably mediates the hydrolysis of some nucleoside diphosphate derivatives; Belongs to the Nudix hydrolase family. PCD1 subfamily. (192 aa)
pykAPyruvate kinase II, glucose stimulated; Protein involved in glycolysis, fermentation and anaerobic respiration. (480 aa)
hisBImidazoleglycerolphosphate dehydratase and histidinol-phosphate phosphatase; Protein involved in histidine biosynthetic process. (355 aa)
pdxBErythronate-4-phosphate dehydrogenase; Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily. (378 aa)
talATransaldolase A; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (316 aa)
tktBTransketolase 2, thiamine triphosphate-binding; 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. 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 (By similarity). (667 aa)
rpoSRNA polymerase, sigma S (sigma 38) 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 the master transcriptional regulator of the stationary phase and the general stress response. Controls, positively or negatively, the expression of several hundred genes, which are mainly involved in metabolism, transport, regulation and stress management. (330 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)
rngRibonuclease G; Involved in the processing of the 5'-end of 16S rRNA. Could be involved in chromosome segregation and cell division. It may be one of the components of the cytoplasmic axial filaments bundles or merely regulate the formation of this structure. Belongs to the RNase E/G family. RNase G subfamily. (489 aa)
phpPhosphotriesterase homology protein; Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate. No enzymatic activity was detected with any of these non-specific substrates. (292 aa)
gphPhosphoglycolate phosphatase; Specifically catalyzes the dephosphorylation of 2- phosphoglycolate (2P-Gly). Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'- phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress; Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. (252 aa)
aroB3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). (362 aa)
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. (309 aa)
ilvAL-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)
yigLPyridoxal phosphate phosphatase; Catalyzes Strongly the dephosphorylation of pyridoxal- phosphate (PLP) and moderately the dephosphorylation of 2-deoxyglucose 6-phosphate (2bGLU6P) and beta-glucose 6-phosphate (bGlu6P). Also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates. (266 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)
metLBifunctional aspartokinase/homoserine dehydrogenase 2; Aspartokinase II and homoserine dehydrogenase II; Protein involved in methionine biosynthetic process and homoserine biosynthetic process. (810 aa)
rpoCRNA polymerase, beta prime subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1407 aa)
pgiGlucosephosphate isomerase; Protein involved in glycolysis and gluconeogenesis; Belongs to the GPI family. (549 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)
yjbQThiamine phosphate synthase; Belongs to the UPF0047 family. (138 aa)
nadRTrifunctional NAD biosynthesis/regulator protein NadR; This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity [...] (410 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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