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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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aesAcetyl esterase; Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity. (322 aa)    
Predicted Functional Partners:
nuoC
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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
    
   0.917
ADO47707.1
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.
   
 
 0.768
ADO46494.1
PFAM: peptidase M16 domain protein; KEGG: kpu:KP1_5218 putative peptidase.
    
 
 0.762
ADO47706.1
NADH-quinone oxidoreductase, F subunit; 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.
    
   0.749
ADO47705.1
KEGG: kva:Kvar_1378 NADH-quinone oxidoreductase, E subunit; TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit.
    
   0.748
caiB
L-carnitine dehydratase/bile acid-inducible protein F; Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L- carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA. Belongs to the CoA-transferase III family. CaiB subfamily.
 
    0.701
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.
    
   0.692
ADO48687.1
KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein.
  
   0.657
caiA
acyl-CoA dehydrogenase domain-containing protein; Catalyzes the reduction of crotonobetainyl-CoA to gamma- butyrobetainyl-CoA; Belongs to the acyl-CoA dehydrogenase family.
 
  
 0.590
ADO48728.1
PFAM: AMP-dependent synthetase and ligase; KEGG: cko:CKO_03346 putative crotonobetaine/carnitine-CoA ligase.
 
 0.587
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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