Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the yellow pigment chrysogine (PubMed:28708398). Pyruvic acid and anthranilic acid are likely substrates for the nonribosomal peptide synthetase chry1/NRPS14, with pyruvic acid adenylated by the first A domain and anthranilic acid by the second (Probable). If pyruvic acid and anthranilic acid are merged and released from chry1/NRPS14 by hydrolysis, a subsequent amidation would lead to 2-pyruvoylaminobenzamide (Probable). This process is probably catalyzed by the amidotransferase chry2 using glutamine as amino donor (Probable). The dehydrogenase chry5 that has a terminal berberine bridge domain for C-N cyclization could catalyze the cyclization of 2-pyruvoylaminobenzamide to yield acetyl-4(3H)-quinazolidinone (Probable). A final reduction of acetyl-4(3H)-quinazolidinone catalyzed by the oxidoreductase chry4 would result in chrysogine (Probable). Pigment biosynthesis. Expression is induced during the infection of wheat and barley. 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. VerP has the following architecture: A-T-C-A-T-C. Impairs the production of chrysogine. Belongs to the NRP synthetase family.