FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of aurovertins, fungal polyketides that exhibit potent inhibition of adenosine triphosphate synthase (PubMed:26340065). Tha biosynthesis starts with the HR-PKS aurA that selects propionate as the starter unit; synthesizes a hexa-ene chain through the repeated functions of the KR and DH domains in the first six iterations; selectively introduces three alpha-methyl substitutions at C4, C6, and C16 using the S-adensylmethionine-dependent cMET; and shuts off KR and DH in the last three iterations to afford a 1,3,5-triketo portion that can undergo intramolecular cyclization to yield the alpha-pyrone intermediate (PubMed:26340065). AurE may act as a cyclase and enhances the rate of pyrone formation and product release of aurA (PubMed:26340065). The methyltransferase aurB then methylates the C17 hydroxyl group (PubMed:26340065). C17 methylation is required to initiate epoxidation by the downstream monooxygenase aurC (PubMed:26340065). The monooxygenase aurC and the epoxide hydrolase aurD can iteratively transform the terminal triene portion of the methylated precursor into the dioxabicyclo[3.2.1]octane scaffold of aurovertin E. Epoxidation modifications of the precursor occur in two separate steps; bis-epoxidation of the two terminal olefins takes place first, followed by another epoxidation that occurs at C7-C8 after tetrahydrofuran formation (PubMed:26340065). The O-acyltransferase aurG converts aurovertin E to aurovertin A (PubMed:26340065).