Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. 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. 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] kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytanic acid hydroxylation. kcat is 3845 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 1690 min(-1) for arachidonic acid hydroxylation. kcat is 3520 min(-1) for the reduction of cytochrome c. kcat is 37050 min(-1) for the reduction of ferricyanide. Negatively regulated by the transcriptional repressor FatR (PubMed:11574077, PubMed:11734890). Is induced by fatty acids such as oleate, linoleate and phytanate, that bind and displace the FatR repressor (PubMed:11734890). Is also induced by palmitate, likely via another mechanism (PubMed:11574077). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969). In the N-terminal section; belongs to the cytochrome P450 family.