L-ornithine N(5)-monooxygenase; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence (PubMed:23980626). Cochliobolus heterostrophus produces extracellular coprogen-type siderophores including coprogen, neocoprogen I and neocoprogen II, as well as the intracellular siderophore ferricrocin (PubMed:17056706). The role of extracellular siderophores is to supply iron to their producers in planta and the intracellular ferricrocin is required for intracellular iron distribution and storage with a crucial role in ascus and ascospore development (PubMed:17056706, PubMed:17601875). SIDA2 catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores (PubMed:23980626). The assembly of extracellular coprogen-type siderophores is then performed by the nonribosomal peptide synthetase (NRPS) NPS6 whereas the intracellular siderophore ferricrocin is assembled by NPS2 (PubMed:17056706, PubMed:17601875). 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 repressed by the transcription repressor SRE1 under iron replete conditions (PubMed:23980626). Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.