STRINGSTRING
leuA leuA aceE aceE aceF aceF lpd lpd accA accA mhpF mhpF gloB gloB CAR16834.1 CAR16834.1 ybiW ybiW poxB poxB dld dld hchA hchA pykA pykA pps pps pykF pykF ydhZ ydhZ gloA gloA fumA fumA fumC fumC adhE adhE ydbK ydbK ldhA ldhA sfcA sfcA ycdW ycdW yccX yccX ycbL ycbL pflB pflB mqo mqo atoB atoB ackA ackA pta pta accD accD eutE eutE eutI eutI maeB maeB ppc ppc pflD pflD yqeF yqeF yggD yggD glcB glcB tdcE tdcE mdh mdh accB accB accC accC pck pck tiaE tiaE aldB aldB lldD lldD aceB aceB acs acs fumB fumB frdD frdD frdC frdC frdB frdB frdA frdA CAR20769.1 CAR20769.1
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; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (523 aa)
aceEPyruvate dehydrogenase, decarboxylase component E1, thiamin-binding; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (887 aa)
aceFPyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (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)
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)
gloBPutative hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. (251 aa)
CAR16834.1Fumarate hydratase class I, beta subunit, aerobic (Fumarase); Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (550 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)
dldD-lactate dehydrogenase, FAD-binding, NADH independent; Catalyzes the oxidation of D-lactate to pyruvate. Belongs to the quinone-dependent D-lactate dehydrogenase family. (585 aa)
hchAHsp31 molecular chaperone; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), [...] (283 aa)
pykAPyruvate kinase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (480 aa)
ppsPhosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. (792 aa)
pykFPyruvate kinase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (470 aa)
ydhZConserved hypothetical protein; Homologs of previously reported genes of unknown function. (69 aa)
gloAGlyoxalase I, Ni-dependent; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. (135 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
fumCFumarate hydratase (fumarase C),aerobic Class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (467 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; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (329 aa)
sfcAMalate dehydrogenase, (decarboxylating, NAD-requiring) (malic enzyme); Function experimentally demonstrated in the studied species; enzyme; Belongs to the malic enzymes family. (565 aa)
ycdW2-ketoacid reductase; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. (312 aa)
yccXAcylphosphatase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (163 aa)
ycbLPutative metal-binding hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (215 aa)
pflBPyruvate formate lyase I; Function experimentally demonstrated in the studied species; enzyme. (760 aa)
mqoMalate dehydrogenase, FAD/NAD(P)-binding domain; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
atoBacetyl-CoA acetyltransferase; Function experimentally demonstrated in the studied species; carrier; Belongs to the thiolase-like superfamily. Thiolase family. (394 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; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family. (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)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. (883 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)
yqeFAcetyl-CoA acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (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; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. (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; 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. (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); Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily. (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)
aceBMalate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. (533 aa)
acsacetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. (652 aa)
fumBAnaerobic class I fumarate hydratase (fumarase B); Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (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; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa)
frdAFumarate reductase (anaerobic) catalytic and NAD/flavoprotein subunit; Function experimentally demonstrated in the studied species; enzyme. (602 aa)
CAR20769.1Putative CoA transferase; CoA transferase having broad substrate specificity for short- chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Belongs to the 3-oxoacid CoA-transferase family. (513 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.