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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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lpdLipoamide dehydrogenase, E3 component is part of three enzyme complexes. (475 aa)    
Predicted Functional Partners:
aceF
Pyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.999
sucB
Dihydrolipoyltranssuccinase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 0.997
aceE
Pyruvate dehydrogenase, decarboxylase component E1, thiamin-binding; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.997
sucA
2-oxoglutarate decarboxylase, thiamin-requiring.
 
 0.989
VF_1263
Mercuric reductase.
    
 0.965
gcvH
Glycine cleavage complex lipoylprotein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
 
 
 0.960
gcvP
Glycine decarboxylase, PLP-dependent, subunit (protein P) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
  
 0.950
gcvT
Aminomethyltransferase, tetrahydrofolate-dependent, subunit (T protein) of glycine cleavage complex.
 
 0.947
VF_2301
Dihydrolipoamide dehydrogenase.
  
  
 
0.914
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
  
 
 0.912
Your Current Organism:
Aliivibrio fischeri
NCBI taxonomy Id: 312309
Other names: A. fischeri ES114, Aliivibrio fischeri ES114, Vibrio fischeri ES114, Vibrio fischeri str. ES114, Vibrio fischeri strain ES114
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