Protein Family Models

This entry represents the N-terminal domain from 4'- phosphopantetheinyl transferase enzymes. This domain is structurally related to the Pfam:PF01648 domain with which it forms a pseudodimeric arrangement [2]. [1]. 10997907. Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS;. Structure. 2000;8:883-895. [2]. 24963544. Structure, biochemistry, and inhibition of essential 4'-phosphopantetheinyl transferases from two species of Mycobacteria. Vickery CR, Kosa NM, Casavant EP, Duan S, Noel JP, Burkart MD;. ACS Chem Biol. 2014;9:1939-1944. [3]. 22993090. Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria. Halavaty AS, Kim Y, Minasov G, Shuvalova L, Dubrovska I, Winsor J, Zhou M, Onopriyenko O, Skarina T, Papazisi L, Kwon K, Peterson SN, Joachimiak A, Savchenko A, Anderson WF;. Acta Crystallogr D Biol Crystallogr. 2012;68:1359-1370. (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

holo-[acyl-carrier-protein] synthase transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of acyl-carrier-protein (ACP)

Date:

2023-03-01

This HMM models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics.

Date:

2024-05-30

Formerly dpj. This enzyme adds the prosthetic group, phosphopantethiene, to the acyl carrier protein (ACP) apo-enzyme to generate the holo-enzyme. Related phosphopantethiene--protein transferases also exist. There is an orthologous domain in eukaryotic proteins.

Gene:

acpS

Date:

2021-04-27