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Psed_3041 protein (Pseudonocardia dioxanivorans) - STRING interaction network
"Psed_3041" - NADH dehydrogenase in Pseudonocardia dioxanivorans
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
Psed_3041NADH dehydrogenase (ubiquinone) 24 kDa subunit (158 aa)    
Predicted Functional Partners:
Psed_3042
NADH dehydrogenase (quinone) (499 aa)
  0.999
Psed_5564
NADH-quinone oxidoreductase subunit F (450 aa)
  0.999
Psed_0743
NADH dehydrogenase (quinone) (424 aa)
  0.998
Psed_5563
NADH-quinone oxidoreductase subunit G (820 aa)
 
  0.998
nuoC
NAD(P)H-quinone oxidoreductase subunit J; 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 (291 aa)
   
  0.998
nuoD
NAD(P)H-quinone oxidoreductase 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 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 (440 aa)
   
  0.998
Psed_3297
Respiratory-chain NADH dehydrogenase domain 51 kDa subunit (626 aa)
0.996
nuoI
NAD(P)H-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 (188 aa)
 
  0.996
nuoB
NAD(P)H-quinone oxidoreductase 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 (183 aa)
   
  0.995
Psed_3043
Formate dehydrogenase subunit alpha (942 aa)
 
   
  0.995
Your Current Organism:
Pseudonocardia dioxanivorans
NCBI taxonomy Id: 675635
Other names: Actinobispora, Amycolata, P. dioxanivorans, P. dioxanivorans CB1190, Pseudamycolata, Pseudoamycolata, Pseudonocardia, Pseudonocardia dioxanivorans, Pseudonocardia dioxanivorans CB1190, Pseudonocardia dioxanivorans DSM 44775, Pseudonocardia dioxanivorans Mahendra and Alvarez-Cohen 2005, Pseudonocardia dioxanivorans str. CB1190, Pseudonocardia dioxanivorans strain CB1190
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