Functions as a fatty acid monooxygenase (PubMed:8830036, PubMed:11985584). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:11985584). Shows activity toward fatty acids with a chain length of 9-18 carbons with optimum chain lengths of 12-14 carbons (lauric, tridecylic and myristic acids) (PubMed:8830036, PubMed:11985584). Can also use shorter saturated fatty acids with a chain length of 9 or 10 carbons as substrates (PubMed:11985584). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:8830036, PubMed:11985584). an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450] Binds 1 FAD. Binds 1 FMN. Stimulated NADPH--cytochrome reductase activity in the presence of substrate. Inhibited by fatty acid substrates longer than 13 carbons and the degree of inhibition increases with increasing chain length. Optimum pH is 6.5. In the N-terminal section; belongs to the cytochrome P450 family.