Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of coprinoferrin, an acylated tripeptide hydroxamate siderophore (PubMed:31496254). The biosynthesis of coprinoferrin depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase cpf2 (PubMed:31496254). The second step, the acylation of N(5)-hydroxy-L-ornithine to yield N(5)-hexanoyl-N(5)-hydroxyl-L-ornithine is catalyzed by a not yet identified acyltransferase (Probable). Finally, assembly of coprinoferrin is catalyzed by the nonribosomal peptide synthase (NRPS) cpf1 via amide bond formation between three N(5)-hexanoyl-N(5)-hydroxyl-L-ornithine molecules to release the linear trimer (PubMed:31496254). Interestingly, proteins seemingly not directly related to biosynthesis, such as transcription factors, replication factors, and autophagy-related proteins, are conserved among the clusters homologous to the coprinoferrin cluster, suggesting that the cluster may also play developmental and cell biological functions (Probable). Siderophore biosynthesis. 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, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase. Cpf1 has the following architecture: A-T-C-T-C-T-C. Abolishes the production of coprinoferrin and fails to form fruiting bodies. Belongs to the NRP synthetase family.