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Dehly_0839 protein (Dehalogenimonas lykanthroporepellens) - STRING interaction network
"Dehly_0839" - Proton-translocating NADH-quinone oxidoreductase subunit L in Dehalogenimonas lykanthroporepellens
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Dehly_0839Proton-translocating NADH-quinone oxidoreductase subunit L (653 aa)    
Predicted Functional Partners:
nuoD
NADH dehydrogenase I subunit 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 (367 aa)
 
  0.999
Dehly_0833
NADH dehydrogenase 24 kDa subunit (150 aa)
 
  0.999
nuoH
NADH dehydrogenase; 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 (351 aa)
 
  0.999
Dehly_0840
Proton-translocating NADH-quinone oxidoreductase subunit M (498 aa)
 
0.999
nuoA
NADH-ubiquinone/plastoquinone oxidoreductase subunit 3; 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 (124 aa)
 
  0.999
nuoK
NADH-ubiquinone oxidoreductase subunit 4L; 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 (104 aa)
 
  0.999
nuoB
NADH-quinone oxidoreductase 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 (203 aa)
 
  0.999
nuoN
Proton-translocating NADH-quinone oxidoreductase 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 (486 aa)
0.999
Dehly_0836
4Fe-4S ferredoxin (193 aa)
 
  0.999
Dehly_0624
NADH dehydrogenase (624 aa)
   
  0.999
Your Current Organism:
Dehalogenimonas lykanthroporepellens
NCBI taxonomy Id: 552811
Other names: Chloroflexi bacterium BL-DC-8, Chloroflexi bacterium BL-DC-9, D. lykanthroporepellens, D. lykanthroporepellens BL-DC-9, Dehalogenimonas, Dehalogenimonas lykanthroporepellens, Dehalogenimonas lykanthroporepellens BL-DC-9, Dehalogenimonas lykanthroporepellens str. BL-DC-9, Dehalogenimonas lykanthroporepellens strain BL-DC-9
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