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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
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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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Psed_3136Hydrolase; KEGG: scb:SCAB_1521 hydrolase. (307 aa)    
Predicted Functional Partners:
Psed_3297
KEGG: scb:SCAB_16891 respiratory chain oxidoreductase; PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; NADH:ubiquinone oxidoreductase, 24kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; SMART: NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding.
    
   0.791
nuoI
NAD(P)H-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.
  
 
 0.542
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
   
 
 0.532
Psed_5563
NADH-quinone oxidoreductase, 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.
   
 
 0.527
nuoB
NAD(P)H-quinone oxidoreductase subunit K; 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.
    
   0.445
Psed_2755
Rieske (2Fe-2S) iron-sulfur domain protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: sen:SACE_1686 ubiquinol-cytochrome c reductase iron-sulfur subunit.
   
 
 0.437
Psed_4723
PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: tcu:Tcur_2193 Rieske (2Fe-2S) domain-containing protein.
   
 
 0.437
Psed_3135
TIGRFAM: Conserved hypothetical protein CHP03083, actinobacterial-type; KEGG: mav:MAV_0227 hypothetical protein.
       0.427
nuoA
NAD(P)H-quinone 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 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 subunit 3 family.
    
   0.427
Psed_0252
Amino acid adenylation domain protein; SMART: Polyketide synthase, phosphopantetheine-binding; Polyketide synthase, thioesterase domain; TIGRFAM: Amino acid adenylation; Non-ribosomal peptide synthase; KEGG: msm:MSMEG_0019 amino acid adenylation; PFAM: AMP-dependent synthetase/ligase; Phosphopantetheine-binding; Condensation domain; Thioesterase.
  
 0.424
Your Current Organism:
Pseudonocardia dioxanivorans
NCBI taxonomy Id: 675635
Other names: P. dioxanivorans CB1190, Pseudonocardia dioxanivorans CB1190, Pseudonocardia dioxanivorans DSM 44775, Pseudonocardia dioxanivorans str. CB1190, Pseudonocardia dioxanivorans strain CB1190
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