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fdhF fdhF ynfE ynfE ynfF ynfF torZ torZ narG narG narZ narZ fdnG fdnG ydeP ydeP torA torA dmsA dmsA napA napA nuoG nuoG fdoG fdoG bisC bisC
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:
fdhFFormate dehydrogenase-H, selenopolypeptide subunit; Function experimentally demonstrated in the studied genus; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (715 aa)
ynfEOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (808 aa)
ynfFOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (807 aa)
torZTrimethylamine N-oxide reductase system III, catalytic subunit; Function experimentally demonstrated in the studied species; enzyme. (809 aa)
narGNitrate reductase 1, alpha subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1247 aa)
narZNitrate reductase 2 (NRZ), alpha subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1246 aa)
fdnGFormate dehydrogenase-N, alpha subunit, nitrate-inducible; Function experimentally demonstrated in the studied genus; enzyme. (1015 aa)
ydePPutative oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 aa)
torATrimethylamine N-oxide (TMAO) reductase I, catalytic subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (848 aa)
dmsADimethyl sulfoxide reductase, anaerobic, subunit A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (814 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. (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. 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. Belongs to the complex I 75 kDa subunit family. (910 aa)
fdoGFormate dehydrogenase-O, large subunit; Function experimentally demonstrated in the studied genus; enzyme. (1016 aa)
bisCBiotin sulfoxide reductase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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