Cytochrome P450 monooxygenase; part of the gene cluster A that mediates the biosynthesis of botcinic acid and its botcinin derivatives, acetate-derived polyketides that contribute to virulence when combined with the sesquiterpene botrydial. Botcinic acid and its derivatives have been shown to induce chlorosis and necrosis during host plant infection, but also have antifungal activities. Two polyketide synthases, BOA6 and BOA9, are involved in the biosynthesis of botcinins. BOA6 mediates the formation of the per-methylated tetraketide core by condensation of four units of malonyl-CoA with one unit of acetyl-CoA, which would be methylated in activated methylene groups to yield a bicyclic acid intermediate that could then either be converted to botrylactone derivatives or lose the starter acetate unit through a retro-Claisen type C-C bond cleavage to yield botcinin derivatives. The second polyketide synthase, BOA9, is probably required for the biosynthesis of the tetraketide side chain of botcinins (Probable). The methyltransferase (MT) domain within BOA6 is probably responsible for the incorporation of four methyl groups (Probable). The trans-enoyl reductase BOA5 might take over the enoyl reductase function of BOA6 that misses an ER domain (Probable). The monooxygenases BOA2, BOA3 and BOA4 might be involved in further hydroxylations at C4, C5 and C8, whereas BOA7, close to BOA9, could potentially be involved in the hydroxylation at C4 in the side chain of botcinins (Probable)