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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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Edges represent protein-protein associations
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[Homology]
Score
ndh1Probable NADH dehydrogenase. Homology to ndh of P. fluorescens of 48% (trembl|Q9KGX0). TRANSFER OF ELECTRONS FROM NADH TO THE RESPIRATORY CHAIN. THE IMMEDIATE ELECTRON ACCEPTOR FOR THE ENZYME IS BELIEVED TO BE UBIQUINONE. DOES NOT COUPLE THE REDOX REACTION TO PROTON TRANSLOCATION. Interpro: FAD-dependent pyridine nucleotide-dislphide oxidoreductase (IPR001327) Pfam: Pyridine nucleotide-disluphide oxidoreductase no signal peptide no TMHs; Family membership. (498 aa)    
Predicted Functional Partners:
hoxF
Probable hydrogen dehydrogenase, alpha subunit. Homology to hoxF of A. eutrophus of 41% (sprot|HOXF_ALCEU). SUBUNITS ALPHA AND GAMMA OF HOXS CONSTITUTE AN NADH-OXIDOREDUCTASE. InterPro: Respiratory-chain NADH dehydrogenase 51 Kd subunit (IPR001949); Respiratory-chain NADH dehydrogenase 24 Kd subunit (IPR002023) Pfam: Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit no signal peptide no TMHs; High confidence in function and specificity.
     
 0.871
fdh1B
Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity.
     
 0.871
nuoL
NADH-ubiquinone oxidoreductase, chain L probable; NADH-quinone oxidoreductase chain L (EC 1.6.99.5) (NADH dehydrogenase I chain L) (NDH-1 chain L). 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 (By similarity). 2A0310: [...]
  
 
 0.787
boxA
Benzoyl-CoA oxygenase component A. 84% 4Fe4S_ferredoxin. IPR001709; FPN_cyt_redctse. IPR001433; Oxred_FAD/NAD(P). Pfam:PF00037; Fer4; 2. PF00175; NAD_binding_1; 1; High confidence in function and specificity.
     
 0.752
nuoA
Putative NADH-ubiquinone oxidoreductase 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.
   
 
 0.736
nuoM
Putative NADH-ubiquinone oxidoreductase, chain M; NADH-quinone oxidoreductase chain M (EC 1.6.99.5) (NADH dehydrogenase I chain M) (NDH-1 chain M). 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. InterPro: NADH-Ubiquino [...]
   
 
 0.735
nuoH
Putative NADH-ubiquinone oxidoreductase chain 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.
   
 
 0.734
nuoK
Putative NADH-ubiquinone oxidoreductase, chain 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 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 4L family.
   
 
 0.732
nuoC
Respiratory-chain NADH dehydrogenase, chain C probable; 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.
     
 0.730
nuoD
Putative NADH-ubiquinone oxidoreductase chain 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.
     
 0.730
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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