PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of isoflavipucine (PubMed:21236704). The PKS part of the PKS-NRPS ATEG_00325 probably assembles a triketide from an acetyl starter and two malonyl-CoA extender units (PubMed:21236704). The poly-beta-keto intermediate would then be fused to the leucine unit by the NRPS part (PubMed:21236704). The resulting amide would be liberated from the PKS-NRPS through reductive release of the linear PKS-NRPS product from the enzyme complex (PubMed:21236704). Further steps in isoflapucine synthesis include a cyclization step, an oxidation step, a hydrolysis step involving a trans-amidation, and an additional oxidation step, leading to flavipucine (PubMed:21236704). Formation of isoflavipucine from flavipucine requires an unusual rearrangement (PubMed:21236704). Alternative rearrangement reactions could build up rubrobramide, representing a branching of flavipucine biosynthesis (PubMed:21236704). The enzymes involved in the post-PKS-NRPS steps have not been identified yet, but the putative oxygenases ATEG_003329 and ATEG_00330 encoded by the cluster could play a role (PubMed:21236704). Expression is inhibited by various sugars, including glucose, fructose, mannose, and ribose (PubMed:21236704). Expression is repressed by the carbon catabolite repressor creA (PubMed:21236704). Expression is increased at alkaline pH in a pacC dependent manner, but glucose repression dominates the effect of alkalization (PubMed:21236704). Nitrogen sources such as amino acids Asn or Gln can also activate expression (PubMed:21236704). Finally, expression is positively controled by the cluster-specific regulator ATEG_00326 (PubMed:21236704). 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 (PubMed:21236704). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (PubMed:21236704). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) or reductase domain (R) that releases the newly synthesized peptide from the enzyme (PubMed:21236704). ATEG_00325 contains also a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a dehydratase domain (DH), a methyltransferase (MT) domain, a ketoreductase domains (KR), and an acyl carrier (ACP) domain (PubMed:21236704). ATEG_00325 has the following architecture: KS-AT-DH-MT-KR-ACP-C-A-T-R/C (PubMed:21236704). The DH, MT and KR domains seem not to contribute to biosynthesis (PubMed:21236704). Abolishes the production of isoflavipucine and dihydroisoflavipucine (PubMed:21236704). In the C-terminal section; belongs to the NRP synthetase family.