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STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
aoxAArsenite oxidase, small subunit; Function of strongly homologous gene; enzyme. (174 aa)    
Predicted Functional Partners:
nuoCD
NADH-quinone oxidoreductase, subunits C and D; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
   
 
 0.997
aoxB
Arsenite oxidase, large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
 
  
 0.997
qcrB
Quinol-cytochrome c reductase, fused cytochrome b/c subunit; Function of strongly homologous gene; carrier.
  
 0.994
NIDE0899
Putative Quinol-cytochrome c reductase, cytochrome b subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier.
 
 0.980
nuoE
NADH-quinone oxidoreductase, subunit E; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 
 0.939
fdsG
Formate dehydrogenase, gamma subunit; Function of strongly homologous gene; enzyme.
   
 
 0.939
nuoD
NADH-quinone oxidoreductase, subunit D; 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; Belongs to the complex I 49 kDa subunit family.
   
 
 0.938
nuoC
NADH-quinone oxidoreductase, subunit C; 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; Belongs to the complex I 30 kDa subunit family.
   
 
 0.922
nuoI
NADH-quinone oxidoreductase, subunit I (modular protein); 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.
  
 
 0.919
nuoI-2
NADH-quinone oxidoreductase, subunit I; 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.
  
 
 0.919
Your Current Organism:
Nitrospira defluvii
NCBI taxonomy Id: 330214
Other names: Candidatus Nitrospira defluvii, LMG 27402, LMG:27402, N. defluvii, NCIMB 14950, strain A17
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