CATH Classification

Domain Context

CATH Clusters

Superfamily 4'-phosphopantetheinyl transferase domain
Functional Family Holo-[acyl-carrier-protein] synthase

Enzyme Information
Holo-[acyl-carrier-protein] synthase.
based on mapping to UniProt P24224
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 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

UniProtKB Entries (1)

Escherichia coli K-12
Holo-[acyl-carrier-protein] synthase

PDB Structure

External Links
Primary Citation
Structure, High Affinity, and Negative Cooperativity of the Escherichia coli Holo-(Acyl Carrier Protein):Holo-(Acyl Carrier Protein) Synthase Complex.
Marcella, A.M., Culbertson, S.J., Shogren-Knaak, M.A., Barb, A.W.
J. Mol. Biol.