Member database | SUPERFAMILY |
SUPERFAMILY type | homologous superfamily |
Description Imported from IPR037143
The 4'-phosphopantetheinyl transferase domain superfamily of proteins transfer the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pp-binding. 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 ACPS_ECOLI and the Sfp type such as SFP_BACSU. The structure of the Sfp type is known
[2], which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
References Imported from IPR037143
1.Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. Lambalot RH, Walsh CT. J. Biol. Chem. 270, 24658-61, (1995). View articlePMID: 7559576
2.Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily. Reuter K, Mofid MR, Marahiel MA, Ficner R. EMBO J. 18, 6823-31, (1999). View articlePMID: 10581256