Protein Family Models

This domain is found at the N-terminal end of human 4'-phosphopantetheinyl transferase (also known as L-aminoadipate -semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASDHPPT), which catalyses the post-translational modification of target proteins by phosphopantetheine. This protein consists of two nearly identical domains (this entry and Pfam:PF01648) connected by a short linker region. Both domains show a pair of beta-sheets connected by a loop region [2]. Paper describing PDB structure 1qr0. [1]. 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. Paper describing PDB structure 2byd. [2]. 18022563. Mechanism and substrate recognition of human holo ACP synthase. Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U;. Chem Biol. 2007;14:1243-1253. Paper describing PDB structure 4mrt. [3]. 24704508. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification. Tufar P, Rahighi S, Kraas FI, Kirchner DK, Lohr F, Henrich E, Kopke J, Dikic I, Guntert P, Marahiel MA, Dotsch V;. Chem Biol. 2014;21:552-562. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

4-phosphopantetheinyl transferase family protein containing an ACPS (holo-[ACP] synthase) domain; ACPS transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of an acyl-carrier-protein (ACP)

Date:

2024-08-06