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lgoD lgoD yahK yahK frmA frmA ybdR ybdR ycjQ ycjQ curA curA adhP adhP rspB rspB ydjJ ydjJ ydjL ydjL gatD gatD yphC yphC acuI acuI tdh tdh qorA qorA groS groS idnD idnD ahr ahr yggP yggP
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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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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
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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
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textmining
co-expression
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Your Input:
lgoDL-galactonate oxidoreductase; Catalyzes the oxidation of L-galactonate to D-tagaturonate. Required for growth on L-galactonate as the sole carbon source. In vitro, can also use L-gulonate. (340 aa)
yahKBroad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined. Belongs to the zinc-containing alcohol dehydrogenase family. (349 aa)
frmAAlcohol dehydrogenase class III; Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (369 aa)
ybdRPutative oxidoreductase. (412 aa)
ycjQPutative Zn-dependent NAD(P)-binding oxidoreductase; Catalyzes the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-gulosides leading to 3-dehydro-D-gulosides. Probably functions in a metabolic pathway that transforms D-gulosides to D- glucosides. Is also able to catalyze the reverse reactions, i.e. the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D- gulosides leading to D-gulosides. In vitro, can oxidize D-gulose and methyl beta-D-guloside, and reduce methyl alpha-3-dehydro-D-guloside and methyl beta-3-dehydro-D-guloside. However, the actual specific physiol [...] (350 aa)
curACurcumin/dihydrocurcumin reductase, NADPH-dependent; Catalyzes the metal-independent reduction of curcumin to dihydrocurcumin (DHC) as an intermediate product, followed by further reduction to tetrahydrocurcumin (THC) as an end product. It also acts on 3-octene-2-one, 3-hepten-2-one, resveratrol, and trans-2-octenal. Belongs to the NADP-dependent oxidoreductase L4BD family. (345 aa)
adhPEthanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. (336 aa)
rspBStarvation-sensing protein RspB; Not known; probable catabolic enzyme. (339 aa)
ydjJPutative oxidoreductase. (347 aa)
ydjLPutative Zn-dependent NAD(P)-binding oxidoreductase. (358 aa)
gatDGalactitol-1-phosphate dehydrogenase, Zn-dependent and NAD(P)-binding; Converts galactitol 1-phosphate to D-tagatose 6-phosphate. Belongs to the zinc-containing alcohol dehydrogenase family. (346 aa)
yphCPutative oxidoreductase. (353 aa)
acuIPutative acryloyl-CoA reductase; Probably catalyzes the NADPH-dependent reduction of acrylyl- CoA to propanoyl-CoA; Belongs to the zinc-containing alcohol dehydrogenase family. Acrylyl-CoA reductase subfamily. (324 aa)
tdhL-threonine 3-dehydrogenase, NAD(P)-binding; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). Belongs to the zinc-containing alcohol dehydrogenase family. (341 aa)
qorAQuinone oxidoreductase, NADPH-dependent; Quinone oxidoreductase; Protein involved in electron carrier activity. (327 aa)
groSCpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. (97 aa)
idnDL-idonate 5-dehydrogenase, NAD-binding; Catalyzes the NADH/NADPH-dependent oxidation of L-idonate to 5-ketogluconate (5KG); Belongs to the zinc-containing alcohol dehydrogenase family. (343 aa)
ahrBroad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. (339 aa)
yggPPutative Zn-binding dehydrogenase; To K.pneumoniae SorE. (425 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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