STRINGSTRING
leuA leuA aceE aceE aceF aceF lpd lpd accA accA gloB gloB mhpF mhpF ybiW ybiW poxB poxB pflB pflB ycbL ycbL yccX yccX ycdW ycdW adhE adhE ydbK ydbK ldhA ldhA aldA aldA sfcA sfcA CAQ98346.1 CAQ98346.1 fumC fumC fumA fumA gloA gloA ydhZ ydhZ pykF pykF pps pps pykA pykA hchA hchA dld dld mqo mqo ackA ackA pta pta accD accD eutE eutE eutI eutI maeB maeB yqeF yqeF yggD yggD glcB glcB tdcE tdcE mdh mdh accB accB accC accC pck pck tiaE tiaE aldB aldB lldD lldD pflD pflD ppc ppc aceB aceB acs acs fumB fumB frdD frdD frdC frdC frdB frdB frdA frdA
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:
leuA2-isopropylmalate synthase; Function experimentally demonstrated in the studied species; enzyme. (523 aa)
aceEPyruvate dehydrogenase, decarboxylase component E1, thiamin-binding; Function experimentally demonstrated in the studied species; enzyme. (887 aa)
aceFPyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; Function experimentally demonstrated in the studied species; enzyme. (630 aa)
lpdLipoamide dehydrogenase, E3 component is part of three enzyme complexes; Function experimentally demonstrated in the studied species; enzyme. (474 aa)
accAacetyl-CoA carboxylase, carboxytransferase, alpha subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. (319 aa)
gloBPutative hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. (251 aa)
mhpFacetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds. (316 aa)
ybiWPutative glycyl radical cofactor protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (810 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)
pflBPyruvate formate lyase I; Function experimentally demonstrated in the studied species; enzyme. (760 aa)
ycbLPutative metal-binding hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (215 aa)
yccXAcylphosphatase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (163 aa)
ycdW2-ketoacid reductase; Function experimentally demonstrated in the studied species; enzyme. (312 aa)
adhEFused acetaldehyde-CoA dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (891 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)
ldhAFermentative D-lactate dehydrogenase, NAD-dependent; Function experimentally demonstrated in the studied species; enzyme. (329 aa)
aldAAldehyde dehydrogenase A, NAD-linked; Function experimentally demonstrated in the studied species; enzyme. (479 aa)
sfcAMalate dehydrogenase, (decarboxylating, NAD-requiring) (malic enzyme); Function experimentally demonstrated in the studied species; enzyme. (565 aa)
CAQ98346.1Putative acetyl-CoA acetyltransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (401 aa)
fumCFumarate hydratase (fumarase C),aerobic Class II; Function experimentally demonstrated in the studied species; enzyme. (467 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
gloAGlyoxalase I, Ni-dependent; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. (135 aa)
ydhZConserved hypothetical protein; Homologs of previously reported genes of unknown function. (69 aa)
pykFPyruvate kinase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (470 aa)
ppsPhosphoenolpyruvate synthase; Function experimentally demonstrated in the studied species; enzyme. (792 aa)
pykAPyruvate kinase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (480 aa)
hchAHsp31 molecular chaperone; Function experimentally demonstrated in the studied species; factor. (283 aa)
dldD-lactate dehydrogenase, FAD-binding, NADH independent; Function experimentally demonstrated in the studied species; enzyme. (571 aa)
mqoMalate dehydrogenase, FAD/NAD(P)-binding domain; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
ackAAcetate kinase A and propionate kinase 2; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. (400 aa)
ptaPhosphate acetyltransferase; Function experimentally demonstrated in the studied species; enzyme. (714 aa)
accDacetyl-CoA carboxylase, beta (carboxyltranferase) subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. Belongs to the AccD/PCCB family. (304 aa)
eutEPutative aldehyde dehydrogenase, ethanolamine utilization protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (467 aa)
eutIPutative phosphotransacetylase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (338 aa)
maeBPutative fused malic enzyme oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (759 aa)
yqeFAcetyl-CoA acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (393 aa)
yggDPutative DNA-binding transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (169 aa)
glcBMalate synthase G; Function experimentally demonstrated in the studied species; enzyme. (723 aa)
tdcEPyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Function experimentally demonstrated in the studied species; enzyme. (764 aa)
mdhMalate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
accBAcetyl CoA carboxylase, BCCP subunit; 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)
accCacetyl-CoA carboxylase, biotin carboxylase subunit; Function experimentally demonstrated in the studied species; enzyme. (449 aa)
pckPhosphoenolpyruvate carboxykinase; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. Belongs to the phosphoenolpyruvate carboxykinase (ATP) family. (540 aa)
tiaE2-oxo-carboxylic acid reductase (glyoxalate reductase) (2-ketoaldonate reductase); Function experimentally demonstrated in the studied species; enzyme. (324 aa)
aldBAldehyde dehydrogenase B; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aldehyde dehydrogenase family. (512 aa)
lldDL-lactate dehydrogenase, FMN-linked; Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain; Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family. (396 aa)
pflDPutative formate acetyltransferase 2 (pyruvate formate lyase II); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (765 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (883 aa)
aceBMalate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. (533 aa)
acsacetyl-CoA synthetase; Function experimentally demonstrated in the studied species; enzyme. (652 aa)
fumBAnaerobic class I fumarate hydratase (fumarase B); Function experimentally demonstrated in the studied species; enzyme. (548 aa)
frdDFumarate reductase (anaerobic), membrane anchor subunit; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (119 aa)
frdCFumarate reductase (anaerobic), membrane anchor subunit; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (131 aa)
frdBFumarate reductase (anaerobic), Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (244 aa)
frdAFumarate reductase (anaerobic) catalytic and NAD/flavoprotein subunit; Function experimentally demonstrated in the studied species; enzyme. (602 aa)
Your Current Organism:
Escherichia coli IAI1
NCBI taxonomy Id: 585034
Other names: E. coli IAI1, Escherichia coli str. IAI1, Escherichia coli strain IAI1
Server load: low (40%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.