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fdnG fdnG dmsA dmsA torA torA narG narG narZ narZ ydeP ydeP ynfE ynfE ynfF ynfF torZ torZ napA napA nuoG nuoG bisC bisC fdoG fdoG fdhF fdhF
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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fdnGFormate dehydrogenase-N, alpha subunit, nitrate-inducible; Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). (1015 aa)
dmsADimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. (814 aa)
torATrimethylamine N-oxide (TMAO) reductase I, catalytic subunit; Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. (848 aa)
narGNitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction. (1247 aa)
narZNitrate reductase 2 (NRZ), alpha subunit; This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1246 aa)
ydePPutative oxidoreductase; Probably involved in acid resistance. Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 aa)
ynfEPutative selenate reductase, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (808 aa)
ynfFS- and N-oxide reductase, A subunit, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. (807 aa)
torZTrimethylamine N-oxide reductase system III, catalytic subunit; Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. Can also reduce other N- and S-oxide compounds such as 4-methylmorpholine-N- oxide and biotin sulfoxide (BSO), but with a lower catalytic efficiency; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (809 aa)
napANitrate reductase, periplasmic, large subunit; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (828 aa)
nuoGNADH:ubiquinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (908 aa)
bisCBiotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. (777 aa)
fdoGFormate dehydrogenase-O, large subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1016 aa)
fdhFFormate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. (715 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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