STRINGSTRING
ABK72066.1 ABK72066.1 nuoG nuoG ABK71308.1 ABK71308.1 ABK75546.1 ABK75546.1 nuoI nuoI nuoD nuoD nuoB nuoB nuoC nuoC nuoA nuoA nuoM nuoM nuoH nuoH
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
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textmining
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protein homology
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ABK72066.1Respiratory-chain NADH dehydrogenase domain, 51 kda subunit; Identified by match to protein family HMM PF01512. (431 aa)    
Predicted Functional Partners:
nuoG
NADH-quinone oxidoreductase, G subunit; 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.
 
 0.991
ABK71308.1
NADH-quinone oxidoreductase chain e; Identified by match to protein family HMM PF01257; match to protein family HMM TIGR01958.
 0.990
ABK75546.1
Formate dehydrogenase, gamma subunit; Identified by similarity to GB:CAA11233.1; match to protein family HMM PF01257.
 
 0.989
nuoI
NADH-quinone oxidoreductase, I subunit; 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 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.
 
 0.974
nuoD
NADH-quinone oxidoreducatase, D subunit; 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; Belongs to the complex I 49 kDa subunit family.
 
 0.972
nuoB
NADH-quinone oxidoreductase, B subunit; 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.
 
 0.966
nuoC
NADH-quinone oxidoreductase 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 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; Belongs to the complex I 30 kDa subunit family.
 
 0.965
nuoA
NADH-quinone oxidoreductase, a subunit; 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; Belongs to the complex I subunit 3 family.
  
 0.965
nuoM
NADH-quinone oxidoreductase, M subunit; Identified by similarity to SP:P50974; match to protein family HMM PF00361; match to protein family HMM TIGR01972.
  
 0.961
nuoH
NADH-quinone oxidoreductase, H subunit; 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 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. This subunit may bind ubiquinone (By similarity).
  
 0.959
Your Current Organism:
Mycolicibacterium smegmatis
NCBI taxonomy Id: 246196
Other names: M. smegmatis MC2 155, Mycobacterium smegmatis MC2 155, Mycolicibacterium smegmatis MC2 155
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