STRINGSTRING
thrC thrC tbpA tbpA ilvI ilvI hemL hemL btuF btuF dxs dxs entF entF ybdL ybdL sucA sucA glmE glmE glmS-2 glmS-2 bioA bioA bioF bioF ybiX ybiX poxB poxB hisC hisC irp-5 irp-5 astC astC sufS sufS malY malY puuE puuE ydbK ydbK gadB gadB dadX dadX pabC pabC ycbX ycbX aspC aspC serC serC menD menD yfbQ yfbQ CAR18579.1 CAR18579.1 dsdA dsdA oxc oxc yfdZ yfdZ eutC eutC iscS iscS glyA glyA gabT gabT CAR18983.1 CAR18983.1 rffA rffA ilvA ilvA ilvG ilvG metB metB yiiM yiiM csdA csdA lysA lysA ygeX ygeX ygfZ ygfZ yliK yliK yggS yggS CAR19590.1 CAR19590.1 metC metC ygjG ygjG tdcB tdcB argD argD yhfS yhfS yhfX yhfX malP malP glgP glgP gadA gadA avtA avtA kbl kbl CAR20303.1 CAR20303.1 dsdA-2 dsdA-2 ilvB ilvB metH metH alr alr tyrB tyrB
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
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
Others
textmining
co-expression
protein homology
Your Input:
thrCThreonine synthase; Function experimentally demonstrated in the studied species; enzyme. (428 aa)
tbpAThiamin transporter subunit; Function experimentally demonstrated in the studied species; transporter. (327 aa)
ilvIAcetolactate synthase III, large subunit; Function experimentally demonstrated in the studied species; enzyme. (574 aa)
hemLGlutamate-1-semialdehyde aminotransferase (aminomutase); Function experimentally demonstrated in the studied species; enzyme. (426 aa)
btuFVitamin B12 transporter subunit: periplasmic-binding component of ABC superfamily; Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC. (266 aa)
dxs1-deoxyxylulose-5-phosphate synthase, thiamine-requiring, 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); Belongs to the transketolase family. DXPS subfamily. (620 aa)
entFEnterobactin synthase multienzyme complex component, ATP-dependent; Function experimentally demonstrated in the studied species; enzyme. (1293 aa)
ybdLMethionine aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (386 aa)
sucA2-oxoglutarate decarboxylase, thiamin-requiring; Function experimentally demonstrated in the studied species; enzyme. (933 aa)
glmEMethylaspartate mutase E chain (Glutamate mutase epsilon subunit); Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). (481 aa)
glmS-2Methylaspartate mutase S chain (Glutamate mutase sigma subunit); Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). (170 aa)
bioA7,8-diaminopelargonic acid synthase, PLP-dependent; Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. (429 aa)
bioF8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. (384 aa)
ybiXConserved hypothetical protein with PKHD hydroxylase domain; Homologs of previously reported genes of unknown function. (225 aa)
poxBPyruvate dehydrogenase (pyruvate oxidase), thiamin-dependent, FAD-binding; Function experimentally demonstrated in the studied species; enzyme; Belongs to the TPP enzyme family. (572 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)
irp-5High-molecular-weight nonribosomal peptide/polyketide synthetase 2 (HMWP2); Function of homologous gene experimentally demonstrated in an other organism; enzyme. (2041 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)
sufSSelenocysteine lyase, PLP-dependent; 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. (406 aa)
malYBifunctional beta-cystathionase, PLP-dependent and regulator of maltose regulon; Function experimentally demonstrated in the studied species; enzyme. (390 aa)
puuEGABA aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (421 aa)
ydbKPutative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (1174 aa)
gadBGlutamate decarboxylase B, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the group II decarboxylase family. (466 aa)
dadXFragment of conserved hypothetical protein (partial); Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (356 aa)
pabC4-amino-4-deoxychorismate lyase component of para-aminobenzoate synthase multienzyme complex; Function experimentally demonstrated in the studied species; enzyme. (269 aa)
ycbXPutative 2Fe-2S cluster-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (369 aa)
aspCAspartate aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (396 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)
menDBifunctional 2-oxoglutarate decarboxylase and SHCHC 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)
yfbQPutative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (405 aa)
CAR18579.1Cystathionine gamma-synthase (CGS) (O-succinylhomoserine (thiol)-lyase). (405 aa)
dsdAD-serine ammonia-lyase; Function experimentally demonstrated in the studied species; enzyme. (443 aa)
oxcPutative oxalyl-CoA decarboxylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TPP enzyme family. (564 aa)
yfdZPutative aminotransferase, PLP-dependent; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (412 aa)
eutCEthanolamine ammonia-lyase, small subunit (light chain); Function experimentally demonstrated in the studied species; enzyme; Belongs to the EutC family. (295 aa)
iscSCysteine 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 and selenium atoms from cysteine and selenocysteine 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. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate; Belongs to the class-V pyr [...] (404 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)
gabT4-aminobutyrate aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (426 aa)
CAR18983.1Putative fused protein: aminotransaminase/transcriptional regulator, GntR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (444 aa)
rffATDP-4-oxo-6-deoxy-D-glucose transaminase; Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D- galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D- Glc4O) and L-glutamate; Belongs to the DegT/DnrJ/EryC1 family. (376 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)
ilvGAcetolactate synthase; Function of strongly homologous gene; enzyme. (548 aa)
metBCystathionine gamma-synthase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (386 aa)
yiiMConserved hypothetical protein; Homologs of previously reported genes of unknown function. (224 aa)
csdACysteine sulfinate desulfinase; Function experimentally demonstrated in the studied species; enzyme. (401 aa)
lysADiaminopimelate decarboxylase, PLP-binding; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (420 aa)
ygeX2,3-diaminopropionate ammonia-lyase; Function experimentally demonstrated in the studied species; enzyme. (398 aa)
ygfZEnzyme component involved in 2-methylthio-6-iodeadenosine formation; Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication; Belongs to the tRNA-modifying YgfZ family. (326 aa)
yliKmethylmalonyl-CoA mutase; Function experimentally demonstrated in the studied species; enzyme. (714 aa)
yggSPutative enzyme; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. (234 aa)
CAR19590.1Putative 8-amino-7-oxononanoate synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (390 aa)
metCCystathionine beta-lyase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (395 aa)
ygjGPutrescine: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. Also functions as a cadaverine transaminase in a a L- lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (468 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)
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)
yhfSConserved hypothetical protein; Homologs of previously reported genes of unknown function. (361 aa)
yhfXPutative amino acid racemase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (387 aa)
malPMaltodextrin phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. (797 aa)
glgPGlycogen phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. (815 aa)
gadAGlutamate decarboxylase A, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the group II decarboxylase family. (466 aa)
avtAValine-pyruvate aminotransferase; Function experimentally demonstrated in the studied species; enzyme. (417 aa)
kblGlycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 aa)
CAR20303.1Putative Aspartate transaminase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (430 aa)
dsdA-2D-serine ammonia-lyase; Function experimentally demonstrated in the studied species; enzyme. (443 aa)
ilvBAcetolactate synthase I, large subunit; Function experimentally demonstrated in the studied species; enzyme. (562 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)
alrAlanine racemase 1, PLP-binding, biosynthetic; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (359 aa)
tyrBTyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (397 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.