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2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase is the 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)
E3 binding domain-containing protein
This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)
2-oxo acid dehydrogenase subunit E2
These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain. [1]. 8487300. Refined crystal structure of the catalytic domain of dihysrolipoyl transacetylase (E2P) from azotobacter vineelandii at 2.6 angstroms resolution. Mattevi A, Obmolova G, Kalk KH, Westphal AH, De Kok A, Hol WG;. J Mol Biol 1993;230:1183-1199. (from Pfam)
biotin/lipoyl-containing protein
This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognise the Glycine cleavage system H proteins. (from Pfam)
dihydrolipoyllysine-residue succinyltransferase
This HMM describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase.
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