Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranoviolin A, a pyranonigrin analog with a C-3 methoxy group (PubMed:33117309). Initially, the PKS portion of pyvA synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA, which is then condensed with the thiolation (T) domain-bound glycine activated by the adenylation (A) domain (PubMed:33117309). The subsequent chain release by Dieckmann condensation (DKC) could be catalyzed by the TE domain present at the C-terminus of pyvA and/or the alpha/beta hydrolase pyvD, installing the tetramic acid moiety (Probable). The FAD-dependent monooxygenase pyvC next epoxidizes one of the olefins of the polyketide part, and the epoxide ring-opening induces the dihydro-gamma-pyrone ring formation (Probable). The cytochrome P450 monooxygeanse pyvB would be responsible for the 2 consecutive reactions, in which the dihydro-gamma-pyrone is oxidized to gamma-pyrone and C-7 is hydroxylated to yield pyranonigrin F (Probable). Finally, the O-methyltransferase pyvH methylates the C-3 hydroxy group to complete the biosynthesis (Probable). Secondary metabolite biosynthesis. The N-terminal part acts as a polyketide synthase and includes a ketosynthase (KS) domain that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) domain that selects and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; an enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm. The C-terminal part acts as an NRP synthetase 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. PynA contains one module and terminates in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Completely abolished the production of pyranoviolin A. In the C-terminal section; belongs to the NRP synthetase family. Extended N-terminus.