STRINGSTRING
frmA frmA ybdR ybdR adhP adhP rspB rspB yahK yahK ydjJ ydjJ ydjL ydjL gatD gatD yphC yphC tdh tdh ahr ahr lgoD lgoD
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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
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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
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textmining
co-expression
protein homology
Your Input:
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)
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)
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)
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)
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)
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)
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)
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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