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ilvI ilvI ilvH ilvH mhpF mhpF sdhC sdhC sdhD sdhD sdhA sdhA sdhB sdhB ybiW ybiW yeaU yeaU ydiF ydiF adhE adhE puuE puuE ydbK ydbK gadB gadB yneI yneI pflB pflB atoD atoD atoA atoA atoB atoB yfcX yfcX gabD gabD gabT gabT ilvM ilvM ilvG ilvG pflD pflD yihU yihU fadB fadB yqeF yqeF tdcE tdcE gadA gadA ilvN ilvN ilvB ilvB frdD frdD frdC frdC frdB frdB frdA frdA CAR20770.1 CAR20770.1
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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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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:
ilvIAcetolactate synthase III, large subunit; Function experimentally demonstrated in the studied species; enzyme. (574 aa)
ilvHAcetolactate synthase III, thiamin-dependent, small subunit; Function experimentally demonstrated in the studied species; enzyme. (163 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)
sdhCSuccinate dehydrogenase, membrane subunit, binds cytochrome b556; Function experimentally demonstrated in the studied species; membrane component. (129 aa)
sdhDSuccinate dehydrogenase, membrane subunit, binds cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
sdhBSuccinate dehydrogenase, FeS subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (238 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)
yeaUPutative tartrate dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (361 aa)
ydiFFragment of putative acyl-CoA dehydrogenase (part 1); 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. (531 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)
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)
yneIPutative aldehyde dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (462 aa)
pflBPyruvate formate lyase I; Function experimentally demonstrated in the studied species; enzyme. (760 aa)
atoDacetyl-CoA:acetoacetyl-CoA transferase, alpha subunit; Function experimentally demonstrated in the studied species; carrier. (220 aa)
atoAacetyl-CoA:acetoacetyl-CoA transferase, beta subunit; Function experimentally demonstrated in the studied species; carrier. (216 aa)
atoBacetyl-CoA acetyltransferase; Function experimentally demonstrated in the studied species; carrier; Belongs to the thiolase-like superfamily. Thiolase family. (394 aa)
yfcXFused enoyl-CoA hydratase and epimerase and isomerase; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (714 aa)
gabDSuccinate-semialdehyde dehydrogenase I, NADP-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aldehyde dehydrogenase family. (482 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)
ilvMAcetolactate synthase II, small subunit; Function experimentally demonstrated in the studied species; enzyme. (87 aa)
ilvGAcetolactate synthase; Function of strongly homologous gene; enzyme. (548 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)
yihUPutative oxidoreductase with NAD(P)-binding Rossmann-fold domain; Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1- sulfonate (DHPS); Belongs to the HIBADH-related family. 3-sulfolactaldehyde reductase subfamily. (298 aa)
fadBEnoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (729 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)
tdcEPyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Function experimentally demonstrated in the studied species; enzyme. (764 aa)
gadAGlutamate decarboxylase A, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the group II decarboxylase family. (466 aa)
ilvNAcetolactate synthase I, small subunit; Function experimentally demonstrated in the studied species; enzyme. (96 aa)
ilvBAcetolactate synthase I, large subunit; Function experimentally demonstrated in the studied species; enzyme. (562 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)
CAR20770.1Putative acyl-CoA hydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the enoyl-CoA hydratase/isomerase family. (258 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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