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nuoC protein (Pedobacter sp. BAL39) - STRING interaction network
"nuoC" - NDH-1 subunit C in Pedobacter sp. BAL39
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Known Interactions
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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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nuoCNDH-1 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 a menaquinone. 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 (167 aa)    
Predicted Functional Partners:
PBAL39_05743
NADH dehydrogenase I, chain B (128 aa)
  0.999
nuoD
NDH-1 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 a menaquinone. 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 (404 aa)
  0.999
nuoI
NDH-1 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 (167 aa)
 
  0.999
nuoH
NDH-1 subunit H ; 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. This subunit may bind ubiquinone (345 aa)
 
  0.999
nuoA
NUO1 ; 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 a menaquinone. 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 (123 aa)
  0.999
PBAL39_05728
NADH dehydrogenase I chain E (170 aa)
 
  0.999
PBAL39_05718
NADH dehydrogenase I chain G (334 aa)
 
  0.999
nuoN
NDH-1 subunit N ; 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 a menaquinone. 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 (457 aa)
 
  0.999
PBAL39_05723
NADH dehydrogenase I chain F (453 aa)
 
  0.998
PBAL39_05693
NADH dehydrogenase I chain L (630 aa)
 
  0.998
Your Current Organism:
Pedobacter sp. BAL39
NCBI taxonomy Id: 391596
Other names: P. sp. BAL39, Pedobacter BAL39, Pedobacter sp. BAL39
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