Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide fusaristatin A (PubMed:25412204). Fusaristatin A consists of a polyketide chain linked to three amino acid residues glutamine (Gln), dehydroalanine (dehydro-Ala), and beta-aminoisobutyric acid (PubMed:25412204). The biosynthesis starts with formation of a linear polyketide chain by the highly reducing polyketide synthase PKS6 (PubMed:25412204). The gene cluster does not contain an acyl-CoA ligase or an acyl-transferase, and it is therefore predicted that the polyketide is transferred directly to the nonribosomal peptide synthetase NRPS7 (Probable). Modules 1-3 from NRPS7 incorporate dehydro-Ala, Gln, and beta-aminoisobutyric acid in the compound, which is released by cyclization (PubMed:25412204). The beta-aminoisobutyric acid units are most likely not freely available to the NRPS, but can be synthesized from thymine, which requires a dehydrogenase, a monooxygenase, and an aminotransferase. The fusaristatin A cluster contains a cytochrome P450 monooxygenase (FGSG_08207) and an aminotransferase (FGSG_17085), which theoretically can perform two of the enzymatic steps (Probable). The enzymes may however also be involved in biosynthesis of dehydroalanine or modification of the polyketide (Probable). The dehydro-Ala residue can be a result of cyclization, where serine is dehydrated (Probable). The last gene of the cluster encodes a protein with an A/B barrel domain found in variable enzymes, which hampers functional prediction (Probable). 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 (By similarity). NRPS7 has the following architecture: C-A-T-C-A-T-C-A-T-Cy. The last condensation domain (Cy) could be responsible for cyclization of the final product (Probable). impairs the production of fusaristatin A. Belongs to the NRP synthetase family.