Dioxygenase; part of the gene cluster that mediates the biosynthesis of chrodrimanin B, a meroterpenoid that acts as a potent blocker of insect GABA-gated chloride channels. The first step of the pathway is the biosynthesis of 6-hydroxymellein by the polyketide synthase cdmE. The prenyltransferase cdmH acts as a 6-hydroxymellein 5-farnesyltransferase and produces the hydrophobic metabolite verruculide C. The FAD-dependent monooxygenase cdmI further converts verruculide C into verruculide B. The terpene cyclase cdmG then produced the pentacyclic molecule 3-hydroxypentacecilide A, the backbone structure of chrodrimanin B, via folding the farnesyl moiety of the substrate into the chair-boat conformation. The short-chain dehydrogenase/reductase cdmF functions as the 3-OH dehydrogenase that oxidizes the C-3 hydroxyl group of 3-hydroxypentacecilide A and produces chrodrimanin C, the dehydrogenated product of 3-hydroxypentacecilide A. The cytochrome P450 monooxygenase cdmJ then accepts both 3-hydroxypentacecilide A and chrodrimanin C and functions as a C-7-beta-hydroxylase to produce respectively chrodrimanin H and chrodrimanin F. The dioxygenase cdmA accepts chrodrimanin H to afford chrodrimanin E, which is further transformed to chrodrimanin A by the dioxygenase cdmD. CdmA can also accept chrodrimanin C as substrate to convert it into verruculide A, which is further converted into chrodrimanin T by cdmD. The last step of the biosynthesis is proposed to be performed by the acetyltransferase cdmC which acetylates chrodrimanin A to yield chrodrimanin B (Probable). The pathway may also lead to the production of additional shunt products, including chrodrimanins T and U