Protein Family Models

Date:

2024-08-14

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)

Date:

2024-08-14

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)

Date:

2024-08-14

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)

Date:

2024-08-14

This HMM describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model.

Gene:

aceF

Date:

2024-05-29

dihydrolipoyllysine-residue acetyltransferase (E2) component of pyruvate dehydrogenase complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)

Date:

2017-10-30