Pathways & interactions
ACP-like superfamily (IPR036736)
Short name: ACP-like_sf
- D-alanyl carrier protein (IPR003230)
- Acyl carrier protein (ACP) (IPR003231)
- Phosphopantetheine attachment site (IPR006162)
- Phosphopantetheine binding ACP domain (IPR009081)
- 10-formyltetrahydrofolate dehydrogenase (IPR011407)
- L-2-aminoadipate reductase (IPR014397)
- Polyketide synthase, phosphopantetheine-binding domain (IPR020806)
Acyl carrier protein (ACP) is an essential cofactor in the synthesis of fatty acids by the fatty acid synthetases systems in bacteria and plants. In addition to fatty acid synthesis, ACP is also involved in many other reactions that require acyl transfer steps, such as the synthesis of polyketide antibiotics, biotin precursor, membrane-derived oligosaccharides, and activation of toxins, and functions as an essential cofactor in lipoylation of pyruvate and alpha-ketoglutarate dehydrogenase complexes [PMID: 12057197]. Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups [PMID: 18551496]. Phosphopantetheine is attached to a serine residue in these proteins. The core structure of ACP consists of a four-helical bundle, where helix three is shorter than the others.
Several other proteins share structural homology with ACP, such as the bacterial apo-D-alanyl carrier protein, which facilitates the incorporation of D-alanine into lipoteichoic acid by a ligase, necessary for the growth and development of Gram-positive organisms [PMID: 11434765]; and the thioester domain of the bacterial peptide carrier protein (PCP) found within large modular non-ribosomal peptide synthetases, which are responsible for the synthesis of a variety of microbial bioactive peptides [PMID: 10801488].