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HX89_03480 protein (Dermacoccus nishinomiyaensis) - STRING interaction network
"HX89_03480" - NADH dehydrogenase in Dermacoccus nishinomiyaensis
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second shell of interactors
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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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Score
HX89_03480NADH dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (189 aa)    
Predicted Functional Partners:
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 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 (249 aa)
 
  0.999
nuoH
NADH-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 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 (318 aa)
  0.999
HX89_03470
NADH-quinone oxidoreductase subunit; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain (119 aa)
 
  0.999
nuoI
NADH-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 (211 aa)
 
  0.999
HX89_03495
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the complex I subunit 6 family (170 aa)
 
  0.999
nuoD
NADH-quinone oxidoreductase 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 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; Belongs to the complex I 49 kDa subunit family (391 aa)
 
  0.999
HX89_03515
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (505 aa)
 
  0.998
HX89_06115
Ubiquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method- Protein Homology (369 aa)
     
 
  0.887
atpG
ATP synthase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (304 aa)
   
 
  0.858
atpC
ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane (88 aa)
   
   
  0.858
Your Current Organism:
Dermacoccus nishinomiyaensis
NCBI taxonomy Id: 1274
Other names: ATCC 29093, CCM 2140, CCUG 33028, CIP 81.71, D. nishinomiyaensis, DSM 20448, Dermacoccus nishinomiyaensis, Dermacoccus nishinomiyensis, Dermatococcus nishinomiyaensis, Dermatococcus nishinomiyensis, IEGM 393, IFO 15356, JCM 11613, LMG 14222, Micrococcus nishinomiyaensis, Micrococcus nishinomyaensis, NBRC 15356, NCTC 11039
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