Hybrid PKS-NRPS synthetase; part of the hps1-dma1 gene cluster that probably mediates the biosynthesis a derivative of cyclopiazonic acid (CPA) (Probable). The hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) nps1 might incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in the pathway (By similarity). In addition, the cluster also includes the tryptophan dimethylallyltransferase dma1, the FAD-dependent oxidoreductase toxD, the cytochrome P450 monooxygenase cyp3.1 and the methyltransferase DOTSEDRAFT_139328; the latter 2 being not present in all CPA-producing fungi but involved in additional modifications that occur in biosynthesis the of a range of CPA and CPA-like products (Probable). Further studies are required to clarify whether the CPA-like hps1-dma1 cluster is functional or a non-functional relic reflecting evolution of D.septosporum (Probable). Secondary metabolite biosynthesis. Barely expressed under any of the conditions tested. 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, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase. Hps1 contains also a polyketide synthase module (PKS) consisting of several catalytic domains including a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a dehydratase domain (DH), a methyltransferase domain (MT), and a ketoreductase domain (KR). Instead of a thioesterase domain (TE), hps1 finishes with a reductase-like domain (RED) for peptide release. Hps2 has the following architecture: KS-AT-DH-MT-KR-C-A-T-RED. In the C-terminal section; belongs to the NRP synthetase family.