2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the antifungal antibiotic FR901469, an inhibitor of beta-1,3-glucansynthase, exerting antifungal activity against the pathogenes Candida albicans and Aspergillus fumigatus (PubMed:27660098). FR901469 is a cyclic depsipeptide containing 12 amino acid residues and a fatty acid chain (PubMed:27660098). The NRPS frbI contains 12 modules responsible for the formation of the depsipeptide backbone which is denoted as Acyl-Thr-Ala-Tyr-Val-4OHPro-Thr-Thr-3OHPro-threo3OHGln-Gly-Thr-Orn-OH (C71H116N14O23) (Probable). The PKS frbB is probably involved in the production of the hydrocarbon chain, and the acyl-CoA ligase frbC might be involved in the transport of the chain to the peptide ptoduct of frbI (Probable). Because FR901469 contains 3 hydroxylated amino acid residues, the 3 oxygenases frbA, frbH, and frbJ might be participating in amino acid hydroxylation (Probable). As no thioesterase domains were detected in frbI or frbB, the thioesterases frbD and frbE may instead release and cyclize the products of the NRPS and PKS, respectively (Probable). Antifungal biosynthesis. Expression is positively regulated by the cluster-specific transcription factor frbF. FR901469 inhibits the activity of 1,3-beta-glucan synthase from Candida albicans and Aspergillus fumigatus (PubMed:11099224, PubMed:11099225). With minimal inhibitory concentrations (MICs) against Candida albicans and Aspergillus fumigatus of 0.63 ug/ml and 0.16 ug/ml, repectively, FR901469 displays greater inhibitory activity than other 1,3-beta-glucan synthase inhibitors such as, WF11899A, echinocandin B, aculeacin A, and papulacandin B (PubMed:11099224, PubMed:11099225). Belongs to the iron/ascorbate-dependent oxidoreductase family.