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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
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a 3D structure is known or predicted
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[Homology]
Score
AEB83456.1PFAM: 4Fe-4S binding domain; KEGG: ajs:Ajs_3467 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein. (687 aa)    
Predicted Functional Partners:
AEB83452.1
KEGG: dia:Dtpsy_2798 respiratory-chain NADH dehydrogenase domain 51 kDa subunit; 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.
 
 0.999
AEB83453.1
Formate dehydrogenase, alpha subunit; SMART: Molybdopterin oxidoreductase, Fe4S4 domain; TIGRFAM: Formate dehydrogenase, alpha subunit; KEGG: dia:Dtpsy_2797 formate dehydrogenase, alpha subunit; PFAM: Molybdopterin oxidoreductase; Molybdopterin oxidoreductase, Fe4S4 domain; Ferredoxin; 4Fe-4S binding domain; Molydopterin dinucleotide-binding domain; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
 
 
 0.990
AEB85602.1
NADH dehydrogenase (quinone); KEGG: dia:Dtpsy_1386 putative monovalent cation/H+ antiporter subunit A; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; Na+/H+ antiporter MnhB subunit-related protein.
  
 
 0.988
AEB83457.1
KEGG: dia:Dtpsy_2793 cytoplasmic chaperone TorD family protein.
 
  
 0.977
nuoB
NADH-quinone oxidoreductase, B subunit; 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.
  
 0.971
nuoD
NADH dehydrogenase I, D subunit; 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.
  
 0.970
nuoH
NADH dehydrogenase (quinone); 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.
  
 0.969
AEB86223.1
KEGG: app:CAP2UW1_1324 oxidoreductase FAD-binding domain protein; PFAM: Oxidoreductase, FAD-binding domain; Ferredoxin; Cytochrome b/b6, N-terminal; Oxidoreductase FAD/NAD(P)-binding.
  
 
 0.968
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 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.
  
 0.968
nuoC
NADH (or F420H2) 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.
  
 0.968
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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