Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the prenylated pyrroloindoline diketopiperazine acetylaszonalenin (PubMed:19001367). The first step in the pathway is the formation of (R)-benzodiazepinedione by condensation of tryptophan and anthranilic acid catalyzed by the non-ribosomal peptide synthetase anaPS (PubMed:19001367, PubMed:20225828). The prenyltransferase anaPT then converts (R)-benzodiazepinedione to aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via C3-prenylation (PubMed:19001367). The last step in the biosynthesis of acetylaszonalenin via acetylation of aszonalenin at position N1 catalyzed by anaAT (PubMed:19001367). Alkaloid 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, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS12 has the following architecture: A-T-C-A-T-C (PubMed:19001367, PubMed:20225828). The activation and loading of antranilate is performed by the first module (PubMed:20225828). Belongs to the NRP synthetase family.