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HMPREF9018_1237 protein (Prevotella amnii) - STRING interaction network
"HMPREF9018_1237" - Respiratory-chain NADH dehydrogenase, 49 Kd subunit in Prevotella amnii
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Known Interactions
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Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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HMPREF9018_1237Respiratory-chain NADH dehydrogenase, 49 Kd subunit (525 aa)    
Predicted Functional Partners:
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 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 (289 aa)
  0.999
HMPREF9018_1235
4Fe-4S binding domain protein (177 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 (365 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 (116 aa)
 
  0.999
HMPREF9018_1232
Proton-translocating NADH-quinone oxidoreductase, chain L (686 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 (479 aa)
 
  0.999
HMPREF9018_1231
Proton-translocating NADH-quinone oxidoreductase, chain M (503 aa)
 
  0.999
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 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 (102 aa)
   
  0.999
HMPREF9018_1613
Putative acyl carrier protein (85 aa)
     
  0.999
HMPREF9018_1062
Acyl carrier protein ; Carrier of the growing fatty acid chain in fatty acid biosynthesis (78 aa)
     
  0.999
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 679191
Other names: P. amnii, P. amnii CRIS 21A-A, Prevotella amnii, Prevotella amnii CRIS 21A-A, Prevotella amnii Lawson et al. 2008, Prevotella amnii str. CRIS 21A-A, Prevotella amnii strain CRIS 21A-A
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