Fatty-acyl-AMP ligase; part of the gene cluster that mediates the biosynthesis of echinocandin B, a fungal lipidated cyclic hexapeptide that acts as an antifungal agent (PubMed:22998630). Linoleoyl-AMP, produced by the fatty-acyl-AMP ligase ecdI, is transferred to the initiation carrier domain (T0) of ecdA (PubMed:22998630). The linoleoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-ornithine, L-threonine, L-proline, L-homotyrosine, L-threonine, and 4R-methyl-L-proline to form the linear hexapeptide (PubMed:22998630). Thereafter, the terminal condensation (C7) performs macrocyclization of the NRPS product and the cyclic scaffold is released from ecdA (PubMed:22998630). All six of the amino acid residues are hydroxylated, including 4R,5R-dihydroxy-L-ornithine, 4R-hydroxyl-L-proline, 3S,4S-dihydroxy-L-homotyrosine, and 3S-hydroxyl-4S-methyl-L-prolin (PubMed:22998630). In the pathway, all the hydroxylation reactions are proposed to occur following completion of the cyclic peptide, so the unhydroxylated precursor produced by ecdA will undergo six rounds of hydroxylation (PubMed:22998630). Five hydroxylase genes (ecdG, ecdH, ecdK, htyE and htyF) are embedded within the echinocandin B (ecd) and L-homotyrosine (hty) clusters (PubMed:22998630). Antifungal biosynthesis. Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity. Due to their effectiveness as antifungal agents, echinocandin derivatives can be used for the treatment of human invasive candidiasis (PubMed:22998630). Belongs to the ATP-dependent AMP-binding enzyme family.