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JNB_08979 protein (Janibacter sp. HTCC2649) - STRING interaction network
"JNB_08979" - NDH-1 subunit K in Janibacter sp. HTCC2649
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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JNB_08979NDH-1 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)    
Predicted Functional Partners:
JNB_08994
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 (487 aa)
 
  0.999
JNB_08984
NADH dehydrogenase subunit J (269 aa)
 
  0.999
JNB_08974
NADH dehydrogenase subunit L (653 aa)
 
  0.999
JNB_08969
NADH dehydrogenase subunit M (513 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 (524 aa)
 
  0.999
JNB_09014
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 (465 aa)
 
  0.999
JNB_08989
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 (206 aa)
 
  0.999
nuoC
NDH-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 (251 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 (120 aa)
 
  0.998
JNB_09024
NDH-1 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 (198 aa)
 
  0.998
Your Current Organism:
Janibacter sp. HTCC2649
NCBI taxonomy Id: 313589
Other names: J. sp. HTCC2649, Janibacter, Janibacter HTCC2649, Janibacter sp. HTCC2649
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