L-ornithine N(5)-monooxygenase; 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). L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine + NADP(+) L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+) Binds 1 FAD per subunit. Siderophore biosynthesis. Homotetramer. Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.