Nonribosomal peptide synthase; part of the siderophore basidioferrin biosynthetic pathway (PubMed:28842536). The biosynthesis of basidioferrin depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase SMO1 (PubMed:28842536). The second step, the acylation of N(5)-hydroxy-L-ornithine is catalyzed by a not yet identified N-acyltransferase (PubMed:22434909). Finally, assembly of basidioferrin is catalyzed by the nonribosomal peptide synthase (NRPS) NPS2 via amide bond formation between three L-AHO molecules to release the linear L-AHO trimer (PubMed:22434909). N-5-acetyl-N-5-hydroxy-L-ornithine (L-AHO) and N-5-cis-anhydromevalonyl-N-5-hydroxy-L-ornithine (L-AMHO) are accepted as the substrates by the NPS2 adenylation (A) domain, but only L-AHO is trimerized (PubMed:28842536). Siderophore biosynthesis. Expression is induced under iron-depleted conditions (PubMed:28842536). 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 (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). 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 (By similarity). Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase (By similarity). NPS2 has the following architecture: A-T-C-T-C-T-C (PubMed:28842536). Belongs to the NRP synthetase family.