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nuoN protein (Sulfurospirillum deleyianum) - STRING interaction network
"nuoN" - Proton-translocating NADH-quinone oxidoreductase subunit N in Sulfurospirillum deleyianum
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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nuoNProton-translocating NADH-quinone oxidoreductase 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 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 (494 aa)    
Predicted Functional Partners:
nuoH
NADH dehydrogenase (quinone); 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 (330 aa)
 
  0.999
Sdel_0138
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 (132 aa)
 
  0.999
Sdel_0150
Proton-translocating NADH-quinone oxidoreductase subunit M (508 aa)
0.999
nuoC
NADH (or F420H2) 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 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 (266 aa)
 
  0.999
Sdel_0149
Proton-translocating NADH-quinone oxidoreductase subunit L (618 aa)
 
0.999
Sdel_0147
NADH-ubiquinone/plastoquinone oxidoreductase chain 6 (184 aa)
 
  0.999
nuoK
NADH-ubiquinone oxidoreductase chain 4L; 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 (100 aa)
 
  0.999
nuoD
NADH dehydrogenase I 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 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 (408 aa)
 
  0.999
nuoB
NADH-quinone oxidoreductase subunit beta; 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 (169 aa)
 
  0.999
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 (204 aa)
 
  0.999
Your Current Organism:
Sulfurospirillum deleyianum
NCBI taxonomy Id: 525898
Other names: Dehalospirillum, Dehalospirillum Scholz-Muramatsu et al. 2002, Geospirillum, S. deleyianum, S. deleyianum DSM 6946, Sulfurospirillum, Sulfurospirillum deleyianum, Sulfurospirillum deleyianum DSM 6946, Sulfurospirillum deleyianum str. DSM 6946, Sulfurospirillum deleyianum strain DSM 6946
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