STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
nemAChromate reductase, quinone reductase, fmn-linked; Involved in the degradation of toxic compounds Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones . Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response . Catalyzes the reduction of N- ethylmaleimide (NEM) to N-ethylsuccinimide Together with NfsA and NfsB, can use the nitroaromatic explos [...] (365 aa)    
Predicted Functional Partners:
Transcriptional repressor for the nemra-gloa operon, quinone-, glyoxal-, and hocl-activated; Involved in response to both electrophiles and reactive chlorine species (RCS) . Represses the transcription of the nemRA-gloA operon by binding to the NemR box . May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA . Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS . Involved in response to methylglyoxal
Glyoxalase i, ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response
Dihydropteridine reductase, nad(p)h-dependent, oxygen-insensitive; Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4- dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species
Nitroreductase a, nadph-dependent, fmn-dependent; Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli
Rhh-type transcriptional regulator, proline utilization regulon repressor / proline dehydrogenase / delta 1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon
Putative oxidoreductase; May function as oxidoreductase
annotation not available
Lysr family transcriptional regulator, transcriptional activator for ttdabt operon; Positive regulator required for L-tartrate-dependent anaerobic growth on glycerol. Induces expression of the ttdA-ttdB-ygjE operon
Curcumin/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
Broad 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
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 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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