Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications (PubMed:22492455, PubMed:23592999). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA (PubMed:22492455). The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC (PubMed:22492455). The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself (PubMed:22492455). 8 H(+) + holo-[ACP] + 8 malonyl-CoA = atrochrysone carboxyl-[ACP] + 8 CO2 + 8 CoA + 2 H2O Secondary metabolite biosynthesis. Endocrocin is specifically produced in conidia. Expression is positively regulated by the transcription factors brlA and laeA (PubMed:26242966). Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (By similarity). Abolishes the production of endocrocin (PubMed:22492455, PubMed:23592999). Leads to attenuated virulence in a toll-deficient Drosophila invasive aspergillosis model (PubMed:23592999). Endocrocin and related anthraquinones compounds have interesting activities for medicinal uses, including anti-inflammatory activity (PubMed:20379952).