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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
RBY4I_784[S] COG4391 Uncharacterized protein conserved in bacteria. (60 aa)    
Predicted Functional Partners:
fdhB
Formate dehydrogenase, beta subunit; [C] COG4656 Predicted NADH:ubiquinone oxidoreductase, subunit RnfC.
    
   0.897
nuoD
NADH dehydrogenase (quinone), D subunit; 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.
   
   0.856
nuoI
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.
   
   0.854
nuoG
NADH dehydrogenase (quinone), G subunit; 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.
    
   0.844
nuoC
NADH-quinone oxidoreductase chain 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.
   
   0.787
EDZ47195.1
[C] COG3761 NADH:ubiquinone oxidoreductase 17.2 kD subunit.
   
   0.785
petA
Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
   
   0.779
EDZ47467.1
Cytochrome B/c1; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
   
   0.779
EDZ48466.1
protein-L-isoaspartate(D-aspartate) O-methyltransferase; [O] COG2518 Protein-L-isoaspartate carboxylmethyltransferase.
   
   0.768
EDZ48344.1
3-beta hydroxysteroid dehydrogenase/isomerase; [MG] COG0702 Predicted nucleoside-diphosphate-sugar epimerases.
   
   0.767
Your Current Organism:
Rhodobacterales bacterium Y4I
NCBI taxonomy Id: 439496
Other names: R. bacterium Y4I
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