Acyl-carrier-protein synthase that transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein (PubMed:12664133, PubMed:21195204, PubMed:28720735). The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi-domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs) (PubMed:21195204, PubMed:28720735). PptA is able to transfer the cofactor to a broad range of enzymes with acyl- or peptidyl-carrier protein domains and activates target enzymes involved in the synthesis of lysine, but also secondary metabolites including gliotoxin, fumigaclavine C, fumiquinazole A, fumiquinazoline C, pyripyroprene A, fumagillin, the siderophores triacetylfusarinine C (TAFC) and ferricrocin (FC), and dihydroxy naphthalene (DHN)-melanin (PubMed:21195204, PubMed:28720735). Plays an essential role in virulence (PubMed:28720735). apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP] Activity is inhibited bythe antifunfal copmpounds PD 404,182, 6-nitroso-1,2-benzopyrone, and calmidazolium chloride with IC(50) values of 3.9 uM, 35.2 uM, and 19.2 uM, respectively (PubMed:28720735). Leads to the loss of the green conidial pigment and decreased viability of conidia (PubMed:21195204). Impairs virulence in both insect and murine infection models (PubMed:28720735). PptA is a druggable target in Aspergillus species that can be targeted in a selective way (PubMed:28720735). Its combined role in both primary and secondary metabolism, encompassing multiple virulence determinants, makes it a very promising antifungal drug target candidate (PubMed:28720735). Belongs to the P-Pant transferase superfamily.