Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of beauveriolides I and III, cyclodepsipeptides acting as inhibitors of the acyl-CoA:cholesterol acyltransferase (PubMed:31926180). The HR-PKS cm3B initiates the biosynthesis of beauveriolides by iteratively catalyzing the formation of the linear polyketide chain (Probable). The ATP-dependent acetyl-CoA ligase cm3D converts the polyketide carboxylic acid to a CoA thioester which id shuttled to the first T domain in the NRPS cm3A by the acetyltransferase cm3C (Probable). Cm3A contains 13 domains and assembles the polyketide chain, L-phenylalanine, L-alanine, and D-leucine (or D-allo-isoleucine) to form beauveriolide I (or beauveriolide III). The production of both beauveriolides I and III suggests the substrate adaptability of cm3B, using different amino acids as substrates (Probable). Secondary metabolite biosynthesis. Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity. Beauveriolides inhibit selectively the acyl-CoA:cholesterol acyl-transferases (ACATs), leading to blocking the synthesis of cholesteryl esters and decreasing the cholesterol concentration, which suggests that beauveriolides are promising as potential lead compounds for antiatherosclerotic agents (PubMed:14718664, PubMed:19336931). Moreover, this activity correlates with inhibitory activities of beauveriolides in the secretion of amyloid-beta-peptide, which suggests that beauveriolides may be an attractive new candidate for the treatment of Alzheimer's disease (PubMed:19396893). Belongs to the ATP-dependent AMP-binding enzyme family.