STRINGSTRING
ACS41201.1 ACS41201.1 petA petA pqqG pqqG petC petC fdh1B fdh1B nuoG nuoG nuoI nuoI nuoD nuoD nuoC nuoC nuoF nuoF fdh2B fdh2B
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second shell of interactors
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Predicted Interactions
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ACS41201.1Putative protease; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. (431 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.
 
 
 0.987
pqqG
Putative protease; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme.
  
0.970
petC
Ubiquinol-cytochrome c reductase complex, cytochrome c1 subunit; Function of strongly homologous gene; enzyme.
   
 0.967
fdh1B
Tungsten-containing formate dehydrogenase beta subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 
 0.964
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.
   
 
 0.897
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.
  
 
 0.885
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.
   
 
 0.866
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.
   
 
 0.850
nuoF
NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 
 0.842
fdh2B
NAD-dependent formate dehydrogenase, Molybdenum containing, beta subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 
 0.842
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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