Biotin/lipoyl attachment (IPR000089)

Short name: Biotin_lipoyl

Overlapping homologous superfamilies

Domain relationships



The biotin / lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme [PMID: 1526981]. E2 acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group [PMID: 1825611]. The lipoic acid cofactor is found in a variety of proteins that include, H-protein of the glycine cleavage system (GCS), mammalian and yeast pyruvate dehydrogenases and fast migrating protein (FMP) (gene acoC) from Ralstonia eutropha (Alcaligenes eutrophus).

Contributing signatures

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