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ACS42667.1 ACS42667.1 ACS42666.1 ACS42666.1 ACS42668.1 ACS42668.1 ACS42669.1 ACS42669.1 ACS42670.1 ACS42670.1 ACS42671.1 ACS42671.1 nuoL nuoL nuoD nuoD nuoC nuoC nuoB nuoB nuoI nuoI
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ACS42667.1Putative pH adaptation potassium efflux system component (phaF); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (94 aa)    
Predicted Functional Partners:
ACS42666.1
Putative pH adaptation potassium efflux system component (phaG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.998
ACS42668.1
Putative pH adaptation potassium efflux system component(phaE); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.998
ACS42669.1
Putative pH adaptation potassium efflux system component (phaD); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.998
ACS42670.1
Putative pH adaptation potassium efflux system component C; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.998
ACS42671.1
Putative pH adaptation potassium efflux system components A and B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.996
nuoL
NADH-quinone oxidoreductase chain L (NADH dehydrogenase I, chain L); Function of strongly homologous gene; enzyme.
  
 
 0.802
nuoD
NADH-quinone oxidoreductase chain D (NADH dehydrogenase I, chain 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; Belongs to the complex I 49 kDa subunit family.
   
   0.546
nuoC
NADH-quinone oxidoreductase chain C (NADH dehydrogenase I, 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 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; Belongs to the complex I 30 kDa subunit family.
   
   0.546
nuoB
NADH-quinone oxidoreductase chain B (NADH dehydrogenase I, chain 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.
   
   0.546
nuoI
NADH-quinone oxidoreductase subunit I (NADH dehydrogenase I 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.
   
   0.477
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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