Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of the yellow pigment chrysogine (PubMed:29196288). the NRPS chyA mediates the condensation of anthranilic acid and alanine into the intermediate 2-(2-aminopropanamido)benzoic acid (PubMed:29196288). The remainder of the pathway is highly branched yielding at least 13 chrysogine-related compounds (PubMed:29196288). The malonyl transferase chyE converts 2-(2-aminopropanamido)benzoic acid and 2-(2-aminopropanamido)benzamidine into 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 3-((1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)amino)-3-oxopropanoic acid, respectively (PubMed:29196288). ChyD is an amidase, being responsible for the amidation of the carboxylic acid moiety of 2-(2-aminopropanamido)benzoic acid, 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 2-(2-((4-amino-1-carboxy-4-oxobutyl)amino)propanamido)benzoic acid (PubMed:29196288). ChyC is involved in the same reactions as ChyD, but plays a more minor role in the amidation reactions compared to chyD (PubMed:29196288). The oxidoreductases chyH and chyM are involved in oxidation reactions that form N-pyruvoylanthranilamide from 2-(2-aminopropanamido)benzamidine and (1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)glutamine, respectively (PubMed:29196288). N-pyruvoylanthranilamide is further converted via two further branches in the pathway, yielding chrysogine and additional chrysogine-related coumpounds (PubMed:29196288). Chrysogine is likely formed by a spontaneous ring closure from N-pyruvoylanthranilamide (PubMed:29196288). Pigment 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. ChyA has the following architecture: A-T-C-A-T-C. Impairs the production of chrysogine and 13 other chrysogine-related compounds (PubMed:29196288). Belongs to the NRP synthetase family.