Lipoyltransferase/lipoate-protein ligase (IPR004562)

Short name: LipoylTrfase_LipoateP_Ligase

Overlapping homologous superfamilies


Family relationships


Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system. It is covalently attached to a specific lysine residue of the subunit of the complexes.

In mammals, covalent attachment of lipoic acid to the proteins occurs in two successive reactions. First, lipoic acid is activated to lipoyl-AMP by lipoate-activating enzyme, and then the lipoyl moiety is transferred to apoproteins by the action of lipoyltransferase [PMID: 17570395, PMID: 8206978]. In contrast, in Escherichia coli, lipoate-protein ligase A catalyses both the activation and the transfer of lipoate [PMID: 8206909]. This entry includes lipoyltransferases and lipoate-protein ligases.

GO terms

Biological Process

GO:0009249 protein lipoylation

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.