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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
Score
Meso_1410PFAM: ferredoxin; KEGG: mlo:msl0793 ferredoxin. (106 aa)    
Predicted Functional Partners:
Meso_1005
KEGG: mlo:mll0920 hypothetical protein.
  
 0.988
Meso_2428
PFAM: Respiratory-chain NADH dehydrogenase domain, 51 kDa subunit; KEGG: sil:SPO0833 formate dehydrogenase, beta subunit.
  
 0.987
Meso_1782
PFAM: aminotransferase, class V; KEGG: mlo:mlr0015 nitrogenase cofactor synthesis protein nifS.
 
 0.973
nuoI
NADH dehydrogenase 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.
  
 0.945
Meso_1776
FeS assembly scaffold SufA; TIGRFAM: iron-sulfur cluster assembly accessory protein FeS assembly scaffold SufA; PFAM: HesB/YadR/YfhF; KEGG: mlo:mlr0024 HesB-like protein; Belongs to the HesB/IscA family.
 
 0.939
nuoA
NADH dehydrogenase subunit A; 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; Belongs to the complex I subunit 3 family.
   
 0.938
nuoB
NADH dehydrogenase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 (By similarity).
  
 0.938
nuoD
NADH dehydrogenase 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; Belongs to the complex I 49 kDa subunit family.
  
 0.917
nuoC
NADH dehydrogenase subunit C; 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; Belongs to the complex I 30 kDa subunit family.
  
 0.914
Meso_1027
NADH dehydrogenase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
  
 0.898
Your Current Organism:
Chelativorans sp. BNC1
NCBI taxonomy Id: 266779
Other names: C. sp. BNC1, Mesorhizobium sp. BNC1
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