H
IPR037143

4'-phosphopantetheinyl transferase domain superfamily

InterPro entry
Short name4-PPantetheinyl_Trfase_dom_sf
Overlapping entries
 

Description

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

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

GO terms

biological process

  • None

cellular component

  • None

Cross References

Contributing Member Database Entries
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.