Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of Pfam:PF00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP [1]. This superfamily consists of two subtypes: The ACPS type such as Swiss:P24224 and the Sfp type such as Swiss:P39135. The structure of the Sfp type is known [3], which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion. [1]. 7559576. Cloning, overproduction, and characterization of the Escherichia. coli holo-acyl carrier protein synthase.. Lambalot RH, Walsh CT;. J Biol Chem 1995;270:24658-24661.. [2]. 8939709. A new enzyme superfamily - the phosphopantetheinyl transferases.. Lambalot RH, Gehring AM, Flugel RS, Zuber P, LaCelle M, Marahiel. MA, Reid R, Khosla C, Walsh CT;. Chem Biol 1996;3:923-936.. [3]. 10581256. Crystal structure of the surfactin synthetase-activating enzyme. sfp: a prototype of the 4'-phosphopantetheinyl transferase. superfamily [In Process Citation]. Reuter K, Mofid MR, Marahiel MA, Ficner R;. EMBO J 1999;18:6823-6831. (from Pfam)
GO Terms:- Molecular Function:
- magnesium ion binding (GO:0000287)
- Molecular Function:
- holo-[acyl-carrier-protein] synthase activity (GO:0008897)
- Date:
- 2024-08-14