Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:31216742). IliA assembles the backbone of ilicicolin H (PubMed:31216742). The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly (PubMed:31216742). The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate (PubMed:31216742). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H, since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (PubMed:31216742) (Probable). acetyl-CoA + 8 AH2 + ATP + 4 H(+) + holo-[ACP] + L-tyrosine + 7 malonyl-CoA + 2 S-adenosyl-L-methionine = 8 A + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + N-[(4E,6E,10S,12Z,14E)-6,10-dimethyl-3-oxohexadeca-4,6,12,14-tetraenoyl]-L-tyrosyl-[ACP] + 2 S-adenosyl-L-homocysteine Mycotoxin biosynthesis. IliA has the following domain architecture: KS-MAT-DH-MT-KR-ACP-C-A-T-R. The PKS module (domains KS to ACP) is responsible for the biosynthesis of the polyketide chain and catalyzes three Claisen condensations, as well as beta-keto processing and methylation. The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide. The bimodular assembly line is terminated with a putative reductase (R) domain that facilitates formation and release of the tetramic acid product. In the C-terminal section; belongs to the NRP synthetase family.