Beauvericin nonribosomal cyclodepsipeptide synthetase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:25543026, PubMed:27750383, PubMed:28125067). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (By similarity). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclization of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (By similarity). 3 (R)-2-hydroxy-3-methylbutyrate + 6 ATP + 3 L-phenylalanine + 3 S-adenosyl-L-methionine = 6 AMP + beauvericin + 6 diphosphate + 6 H(+) + 3 S-adenosyl-L-homocysteine Expression is highly repressed by the histone deacetylase HDA1 and the beauvericin cluster-specific repressor BEA4 (PubMed:27750383). BEA biosynthesis is also repressed by the activity of the H3K27 methyltransferase KMT6 (PubMed:27750383). 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, additional domains required for further modifications are also present. Beauvericin synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (PubMed:28125067). During catalysis, C3 and C2 take turns to incorporate the two biosynthetic precursors into the growing depsipeptide chain that swings between T1 and T2a/T2b with C3 cyclizing the chain when it reaches the full length (By similarity). Leads to complete loss of beauvericin biosynthesis (PubMed:27750383). Belongs to the NRP synthetase family.