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Slin_5734 protein (Spirosoma linguale) - STRING interaction network
"Slin_5734" - FAD-dependent pyridine nucleotide-disulfide oxidoreductase in Spirosoma linguale
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Known Interactions
from curated databases
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
Slin_5734FAD-dependent pyridine nucleotide-disulfide oxidoreductase (444 aa)    
Predicted Functional Partners:
Slin_5098
NADH-ubiquinone/plastoquinone oxidoreductase chain 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 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 (123 aa)
         
  0.976
Slin_5944
Proton-translocating NADH-quinone oxidoreductase subunit L (642 aa)
       
  0.969
Slin_4909
Proton-translocating NADH-quinone oxidoreductase subunit L (635 aa)
       
  0.969
Slin_6504
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 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 (506 aa)
       
  0.969
Slin_5946
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 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 (467 aa)
       
  0.969
Slin_5099
NADH-quinone oxidoreductase subunit beta; 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 (181 aa)
         
  0.968
Slin_3629
NADH-quinone oxidoreductase subunit beta; 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 (176 aa)
         
  0.968
Slin_5945
Proton-translocating NADH-quinone oxidoreductase subunit M (492 aa)
       
  0.968
Slin_4908
Proton-translocating NADH-quinone oxidoreductase subunit M (559 aa)
       
  0.968
Slin_5103
NADH-quinone oxidoreductase subunit F (446 aa)
         
  0.967
Your Current Organism:
Spirosoma linguale
NCBI taxonomy Id: 504472
Other names: S. linguale, S. linguale DSM 74, Spirosoma, Spirosoma linguale, Spirosoma linguale DSM 74, Spirosoma linguale str. DSM 74, Spirosoma linguale strain DSM 74
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