CATH Classification

Domain Context

CATH Clusters

Superfamily 4'-phosphopantetheinyl transferase domain
Functional Family

Enzyme Information

2.7.8.7
Holo-[acyl-carrier-protein] synthase.
based on mapping to UniProt O25488
CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].
-!- All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. -!- The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain. -!- The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl- carrier and acyl-carrier-proteins from prokaryotes. -!- Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14.

UniProtKB Entries (1)

O25488
ACPS_HELPY
Helicobacter pylori 26695
Holo-[acyl-carrier-protein] synthase

PDB Structure

PDB 5XUK
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structures of acyl carrier protein synthases (AcpS) from three Gram-negative bacteria
Liao, Y.P., Wang, D.L., Yin, D.P., Zhang, Q.Y., Wang, Y.M., Wang, D.Q., Zhu, H.X., Chen, S.
To Be Published