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Mettu_2065 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2065" - Proton-translocating NADH-quinone oxidoreductase, chain M in Methylobacter tundripaludum
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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Mettu_2065Proton-translocating NADH-quinone oxidoreductase, chain M (509 aa)    
Predicted Functional Partners:
nuoC
NDH-1 subunit C/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 (592 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 (389 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 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 (480 aa)
0.997
Mettu_3724
Proton-translocating NADH-quinone oxidoreductase, chain L (609 aa)
 
0.996
nuoK
NDH-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 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 (102 aa)
 
  0.994
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 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 (134 aa)
 
  0.992
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 (171 aa)
 
  0.991
Mettu_3727
NADH-ubiquinone/plastoquinone oxidoreductase chain 6 (172 aa)
 
  0.991
nuoB
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 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 (212 aa)
 
  0.991
Mettu_3730
NADH-quinone oxidoreductase (895 aa)
   
  0.979
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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