Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA, via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable). acetyl-CoA + AH2 + 3 H(+) + 3 malonyl-CoA = A + 3 CO2 + 4 CoA + H2O + orsellinaldehyde Secondary metabolite biosynthesis. Multidomain protein; including an N-terminal starter unit:ACP transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a malonyl-CoA:ACP transacylase (MAT) domain, a product template domain, a acyl carrier protein (ACP) domain, a methyltransferase domain and a reductive NADPH-binding domain that is required for NADPH-dependent product release. Abolishes the production of Aspernidine A.