Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells (PubMed:25302411). The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues (PubMed:25302411). One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine (PubMed:25302411). After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT (PubMed:25302411). In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as tailoring enzymes to produce the intermediate dechloroaspirochlorine (PubMed:25302411). Ultimately, chlorination of dechloroaspirochlorine by the halogenase aclH is the last step in the aspirochlorine pathway (PubMed:25302411). Mycotoxin biosynthesis. Belongs to the cytochrome P450 family.