Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold (PubMed:32182055). The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan (PubMed:32182055). The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B (PubMed:32182055). The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine (PubMed:32182055). The peptide bond formation between the tethered amino acids is catalyzed by the first condensation domain (C1) between anthranilate's carbonyl carbon and kynurenine's aliphatic primary amine (PubMed:32182055). The second C domain (C2) catalyzes the final cyclization event between the aromatic amine of kynurenine and the tethered carbonyl carbon, yielding nanangelenin B (PubMed:32182055). The terminal T3 domain enhances the catalytic efficiency of C2, suggesting the T2-tethered Ant-L-Kyn is transferred to T3 prior to cyclization by C2 (PubMed:32182055). Once released from nanA, nanangelenin B is then prenylated by the prenyltransferase nanD to form nanangelenin C (PubMed:32182055). Nanangelenin C is then N-hydroxylated by the FAD-dependent monooxygenase nanF and further acetylated by the acetyltransferase nanB to yield nanangelenin F (PubMed:32182055). Finally, the N-methyltransferase nanE methylates the amide nitrogen of 1-benzazepine to convert nanangelenin F into nanangelenin A (PubMed:32182055). NanE is also able to methylate most of the intermediates of the pathway such as nanangelenin B and nanangelenin C to produce nanangelenin D and nanangelenin E, respectively (PubMed:32182055). Secondary metabolite 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. NanA has the following architecture: A1-T1-C1-A2-T2-C2-T3. Belongs to the NRP synthetase family.