Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group (PubMed:25859931). The first stage is catalyzed by the nonribosomal pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (By similarity). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (By similarity). PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin (By similarity). The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL (By similarity). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene (PubMed:25859931). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2 (PubMed:25859931). The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD-dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group (PubMed:25859931). The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C (PubMed:25859931, PubMed:28114276). PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D (PubMed:28114276). Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone (PubMed:28114276). Secondary metabolite biosynthesis. Alkaloid biosynthesis. Mycotoxin biosynthesis. NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase. PenN has the following architecture:A-T-C-A-M-T-C. Abolishes the production of penigequinolones A and B. Belongs to the NRP synthetase family.