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
ytfGNAD(P)H:quinone oxidoreductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (297 aa)    
Predicted Functional Partners:
CDX43352.1
Conserved exported hypothetical protein; Homologs of previously reported genes of unknown function.
   
 0.998
nuoD
NADH-quinone oxidoreductase chain D (NADH dehydrogenase I, chain D) (NDH-1, chain 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.
   
 0.995
nuoB
NADH-quinone oxidoreductase chain B (NADH dehydrogenase I, chain B) (NDH-1, chain B); 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.
   
 0.994
CDX43537.1
AMP-dependent synthetase and ligase.
   
 0.989
nuoA
NADH-quinone oxidoreductase chain A (NADH dehydrogenase I, chain A) (NDH-1, chain A); 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 subunit 3 family.
   
 0.988
nuoM
NADH-quinone oxidoreductase chain M (NADH dehydrogenase I, chain M) (NDH-1, chain M); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 0.988
CDX39015.1
Cytochrome c oxidase subunit III.
    
  0.988
CDX39018.1
Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
    
  0.988
ctaD
Cytochrome c oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
    
  0.988
CDX43364.1
Putative cytochrome c oxidase subunit III protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
    
  0.988
Your Current Organism:
Mesorhizobium sp. SOD10
NCBI taxonomy Id: 1505946
Other names: M. sp. SOD10
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