UniProt functional annotation for P0AFG6

UniProt code: P0AFG6.

Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
Function:		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). {ECO:0000305|PubMed:17367808}.
Catalytic activity:		Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)- succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; Evidence={ECO:0000305|PubMed:17367808};
Cofactor:		Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 1 lipoyl cofactor covalently.;
Pathway:		Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subunit:		Forms a 24-polypeptide structural core with octahedral symmetry (PubMed:9677295, PubMed:10739245). Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3) (Probable). Interacts with SucA (via N-terminus), the E1 component of OGDH complex (PubMed:17367808). {ECO:0000269|PubMed:10739245, ECO:0000269|PubMed:17367808, ECO:0000269|PubMed:9677295, ECO:0000305|PubMed:17367808}.
Similarity:		Belongs to the 2-oxoacid dehydrogenase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.