Nonribisomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of benzomalvin A and D (PubMed:28604695). The pathway begins with the loading of amino acid precursors onto the A domains of the non ribosomal peptide synthetases benY and benZ (PubMed:28604695). BenY and the A1 domain of benZ are loaded with anthranilate (Anth), while the A2 domain of benZ is loaded with phenylalanine (Phe) (PubMed:28604695). N-methylation of Phe by the methyltransferase benX may happen before loading of Phe onto benZ, after loading of Phe, or after dipeptide formation (PubMed:28604695). Condensation of Anth with the secondary amine of NmPhe or Phe is catalyzed by the C1 domain of benZ, forming a dipeptide intermediate (PubMed:28604695). This is followed by in trans condensation of the Anth-NmPhe dipeptide with Anth bound to the T domain of benY by the C2 domain of benZ to form the linear tripeptide Anth-NmPhe-Anth (PubMed:28604695). Cyclization and release of the tripeptide is then catalyzed by the C-terminal C domain of benY and the resulting 11-member macrocyclic intermediate is expected to spontaneously collapse to form the benzodiazepine core (PubMed:28604695). Benzomalvin A is in conformational equilibrium with its atropisomer, benzomalvin D (PubMed:28604695). 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. Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase. BenY as the following monomodular architecture: A-T-C. Leads to the accumulation of the benzomalvin dipeptide precursor anthranilate-N-methylphenylalanine (Anth-NmPhe). Belongs to the NRP synthetase family.