L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway (PubMed:26960149). Arthroderma benhamiae produces 2 types of extracellular siderophores, ferrichrome C and ferricrocin (PubMed:26960149). The biosynthesis of these siderophores depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase sidA (PubMed:26960149). The structure of ferricrocin differs from ferrichrome C only by a serine for alanine substitution and the assembly of both siderophores is suggested to be performed by the nonribosomal peptide synthase (NRPS) sidC (PubMed:26960149). 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. Expression is under the control of the iron acquisition regulator hapX (PubMed:26960149). Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.