STRINGSTRING
narI narI fdnI fdnI hyfD hyfD hyfC hyfC hyfB hyfB torY torY ynfH ynfH fdhF fdhF nrfB nrfB nrfA nrfA fdoG fdoG fdoH fdoH fdoI fdoI yhjA yhjA hybO hybO hybA hybA hybB hybB dmsA dmsA dmsB dmsB dmsC dmsC hyaA hyaA hyaB hyaB hyaC hyaC torC torC torA torA narG narG narH narH narV narV narY narY narZ narZ fdnG fdnG fdnH fdnH hybC hybC hycB hycB hycC hycC hycD hycD hycE hycE hycF hycF hycG hycG hyfG hyfG hyfF hyfF hyfE hyfE
Nodes:
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:
a 3D structure is known or predicted
Edges:
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:
narINitrate reductase 1, gamma (cytochrome b(NR)) subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. (225 aa)
fdnIFormate dehydrogenase-N, cytochrome B556 (gamma) 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. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). (217 aa)
hyfDHydrogenase 4, membrane subunit; Possible component of hydrogenase 4. Belongs to the complex I subunit 5 family. (479 aa)
hyfCHydrogenase 4, membrane subunit; Possible component of hydrogenase 4. Belongs to the complex I subunit 1 family. (315 aa)
hyfBHydrogenase 4, membrane subunit; Possible component of hydrogenase 4. (672 aa)
torYTMAO reductase III (TorYZ), cytochrome c-type subunit; Part of the anaerobic respiratory chain of trimethylamine-N- oxide reductase TorZ. Required for electron transfer to the TorZ terminal enzyme. (366 aa)
ynfHOxidoreductase, membrane subunit; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. The C subunit anchors the other two subunits to the membrane and stabilize the catalytic subunits (By similarity); Belongs to the DmsC family. (284 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)
nrfBNitrite reductase, formate-dependent, penta-heme cytochrome c; Plays a role in nitrite reduction. (188 aa)
nrfANitrite reductase, formate-dependent, cytochrome; Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine. Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity). (478 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)
fdoHFormate dehydrogenase-O, Fe-S subunit; Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit (By similarity). (300 aa)
fdoIFormate dehydrogenase-O, cytochrome b556 subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase. (211 aa)
yhjAProtein involved in cytochrome complex assembly. (465 aa)
hybOHydrogenase 2, small subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake; Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family. (372 aa)
hybAHydrogenase 2 4Fe-4S ferredoxin-type component; Participates in the periplasmic electron-transferring activity of hydrogenase 2 during its catalytic turnover. (328 aa)
hybBPutative hydrogenase 2 cytochrome b type component; Probable b-type cytochrome; Belongs to the NrfD family. (392 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)
dmsBDimethyl sulfoxide reductase, anaerobic, subunit B; Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. (205 aa)
dmsCDimethyl sulfoxide reductase, anaerobic, subunit C; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to the membrane and stabilizes it. (287 aa)
hyaAHydrogenase 1, small subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth; Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family. (372 aa)
hyaBHydrogenase 1, large subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (597 aa)
hyaCHydrogenase 1, b-type cytochrome subunit; Probable b-type cytochrome; Belongs to the HupC/HyaC/HydC family. (235 aa)
torCTrimethylamine N-oxide (TMAO) reductase I, cytochrome c-type subunit; Part of the anaerobic respiratory chain of trimethylamine-N- oxide reductase TorA. Acts by transferring electrons from the membranous menaquinones to TorA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of TorC, then from the N-terminus to the C-terminus, and finally to TorA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the TorS kinase activity. (390 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)
narHNitrate reductase 1, beta (Fe-S) subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. (512 aa)
narVNitrate reductase 2 (NRZ), gamma 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. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. (226 aa)
narYNitrate reductase 2 (NRZ), beta 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. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. (514 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)
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)
fdnHFormate dehydrogenase-N, Fe-S (beta) 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 beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, togethe [...] (294 aa)
hybCHydrogenase 2, large subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (567 aa)
hycBHydrogenase 3, Fe-S subunit; Probable electron transfer protein for hydrogenase 3. (203 aa)
hycCMembrane-spanning protein of hydrogenase 3 (part of FHL complex); Protein involved in fermentation; Belongs to the complex I subunit 4 family. (608 aa)
hycDMembrane-spanning protein of hydrogenase 3 (part of FHL complex); Protein involved in fermentation; Belongs to the complex I subunit 1 family. (307 aa)
hycELarge subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family. (569 aa)
hycFFormate hydrogenlyase complex iron-sulfur protein; Probable electron transfer protein for hydrogenase 3. (180 aa)
hycGHydrogenase 3 and formate hydrogenase complex, HycG subunit; Hydrogenase activity; Protein involved in fermentation and anaerobic respiration. (255 aa)
hyfGHydrogenase 4, subunit; Possible component of hydrogenase 4. (555 aa)
hyfFHydrogenase 4, membrane subunit; Possible component of hydrogenase 4. Belongs to the complex I subunit 5 family. (526 aa)
hyfEHydrogenase 4, membrane subunit; Possible component of hydrogenase 4. (216 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
Server load: low (14%) [HD]