Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkylresorcinols called soppilines (PubMed:31086874). The biosynthesis starts with the HR-PKS pspA-catalyzed carbon chain assembly through nine chain elongation cycles, using acetyl CoA and malonyl CoA as a starter and extender units, respectively, to produce the polyketide soppiline A (PubMed:31086874). In the first round, the KR, DH, and CMeT domains work to produce 2-methyl-2-butenyl thioester (PubMed:31086874). In rounds 2 to 5, the KR, DH, and ER domains fully catalyze the reduction of the elongated beta-ketothioester, resulting in the insertion of eight methylene units (PubMed:31086874). The unusual Z,E,Z-triene motif is likely constructed during rounds 6 to 8 (PubMed:31086874). Typically, the DH domain introduces a double bond at an alpha,beta-position of an elongated polyketide chain, with the dehydration of a beta-hydroxy group (PubMed:31086874). The last extension cycle would be carried out with L-oriented beta-ketoreduction by the KR domain to produce beta-hydroxy carboxylic acid soppiline A (PubMed:31086874). The type III PKS pspB intercepts the elongated polyketide chain at round 8 from the HR-PKS pspA, followed by a tri-keto extension and decarboxylative aldol cyclization to produce 1,3,5-trisubstituted alkylresorcinol soppiline B (PubMed:31086874). Subsequently, the cytochrome P450 monooxygenase pspC catalyzes three-step oxidations at the C-4 methyl group to carboxylic acid to yield soppiline C (PubMed:31086874). 3 O2 + 3 reduced [NADPH--hemoprotein reductase] + soppiline B = 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] + soppiline C Secondary metabolite biosynthesis. Belongs to the cytochrome P450 family.