STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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BRADO1504Putative para-nitrobenzyl esterase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (308 aa)    
Predicted Functional Partners:
BRADO1977
Cytochrome b/c1 [Contains: Cytochrome b; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
    
 
 0.776
BRADO6911
Putative lipase/esterase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
     0.623
BRADO1550
Oxydoreductase (2Fe-2S ferredoxin like subunit); Function of strongly homologous gene; enzyme.
    
 
 0.480
nuoG
NADH-quinone oxidoreductase chain G (NADH dehydrogenase I, chain G) (NDH-1, chain G); 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. Belongs to the complex I 75 kDa subunit family.
    
 
 0.480
nuoB
NADH-quinone oxidoreductase chain B (NADH dehydrogenase I, chain B) (NDH-1, chain 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.
    
   0.479
nuoF
NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F) (NDH-1, chain 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.
    
   0.461
fdsB
Putative formate dehydrogenase beta subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
    
   0.461
nuoE
NADH-quinone oxidoreductase chain E (NADH dehydrogenase I, chain E) (NDH-1, chain E); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
    
   0.460
nuoA
NADH-quinone oxidoreductase chain A (NADH dehydrogenase I, chain A) (NDH-1, chain 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.
    
   0.460
fdsG
Putative formate dehydrogenase gamma subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme.
    
   0.460
Your Current Organism:
Bradyrhizobium sp. ORS278
NCBI taxonomy Id: 114615
Other names: B. sp. ORS 278, Bradyrhizobium sp. ORS 278
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