STRINGSTRING
petC petC petA petA petB petB fdh1B fdh1B nuoI nuoI nuoG nuoG nuoD nuoD pqqF pqqF pqqG pqqG ACS41201.1 ACS41201.1 nuoC nuoC
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
petCUbiquinol-cytochrome c reductase complex, cytochrome c1 subunit; Function of strongly homologous gene; enzyme. (297 aa)    
Predicted Functional Partners:
petA
Ubiquinol-cytochrome c reductase complex, iron-sulfur subunit (Rieske iron-sulfur protein); 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.
 
 0.999
petB
Ubiquinol-cytochrome c reductase complex, cytochrome b 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.
 0.999
fdh1B
Tungsten-containing formate dehydrogenase beta subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 
 0.978
nuoI
NADH-quinone oxidoreductase subunit I (NADH dehydrogenase I 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.
  
 
 0.976
nuoG
NADH-quinone oxidoreductase chain G (NADH dehydrogenase I, 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.
  
 
 0.974
nuoD
NADH-quinone oxidoreductase chain D (NADH dehydrogenase I, 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.
  
 
 0.972
pqqF
Putative protease; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme; Belongs to the peptidase M16 family.
   
 0.967
pqqG
Putative protease; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme.
   
 0.967
ACS41201.1
Putative protease; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family.
   
 0.967
nuoC
NADH-quinone oxidoreductase chain C (NADH dehydrogenase I, 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.
   
 
 0.965
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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