Biotin/lipoate A/B protein ligase (IPR004143)

Short name: BPL_LipA_LipB

Domain relationships



This domain is found in biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organism probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine [PMID: 10470036]. Lipoate-protein ligase A (LPLA) (octanoyltransferase) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes [PMID: 8206909].

GO terms

Biological Process

GO:0006464 cellular protein modification process

Molecular Function

GO:0003824 catalytic activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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