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nuoN protein (Nocardioides sp. JS614) - STRING interaction network
"nuoN" - NADH dehydrogenase subunit N in Nocardioides sp. JS614
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experimentally determined
Predicted Interactions
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textmining
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protein homology
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nuoNNADH dehydrogenase 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 (533 aa)    
Predicted Functional Partners:
nuoH
NADH dehydrogenase 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 (449 aa)
 
  0.999
nuoD
NADH dehydrogenase 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 (446 aa)
 
  0.999
nuoC
NADH dehydrogenase 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 (250 aa)
 
  0.999
nuoA
NADH-ubiquinone/plastoquinone oxidoreductase, chain 3; 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 (119 aa)
 
  0.999
nuoK
NADH dehydrogenase subunit K; 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 (99 aa)
 
  0.999
Noca_0529
NADH dehydrogenase subunit J (275 aa)
 
  0.999
Noca_0532
Proton-translocating NADH-quinone oxidoreductase, chain M (509 aa)
0.999
nuoI
NADH dehydrogenase 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 (196 aa)
 
  0.997
nuoB
NADH dehydrogenase subunit 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 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 (184 aa)
 
  0.995
Noca_0526
NADH dehydrogenase subunit G (811 aa)
 
  0.995
Your Current Organism:
Nocardioides sp. JS614
NCBI taxonomy Id: 196162
Other names: N. sp. JS614, Nocardioides, Nocardioides JS614, Nocardioides sp. JS614
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