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biotin/lipoyl-binding protein
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)
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase
This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score.
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