Involved in the degradation of D-nicotine (PubMed:5849820, PubMed:4628374). Catalyzes the oxidation of (R)-6-hydroxynicotine (6-hydroxy-D-nicotine) to 6-hydroxypseudooxynicotine (PubMed:5849820, PubMed:4965794, PubMed:4628374, PubMed:2680607, PubMed:31046245). Oxidation of the pyrrolidine ring of (R)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylmyosmine, which hydrolyzes spontaneously to 6-hydroxypseudooxynicotine (PubMed:4965794, PubMed:4628374, PubMed:31046245). Acts with absolute stereospecificity on the D-form of 6-hydroxynicotine (PubMed:4965794, PubMed:4628374). Shows lower activity with (R)-6-hydroxynornicotine, and weak activity with (R)-4-(1-methylpyrrolidine-2-yl)phenol, (R)-6-chloronicotine and (R)-nicotine (PubMed:31046245). (R)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2 (R)-6-hydroxynicotine + O2 = 6-hydroxy-N-methylmyosmine + H2O2 Binds 1 FAD per subunit (PubMed:4628374, PubMed:16095622). The FAD is covalently bound to the protein (PubMed:4628374, PubMed:5083098, PubMed:2680607, PubMed:2115879, PubMed:16095622). Inhibited by (S)-6-hydroxynicotine (PubMed:5849820, PubMed:4965794, PubMed:4628374). Inhibited by high concentrations of phenanthroline (PubMed:4628374). Fairly stable at neutral or alkaline pH. Inactivated at temperatures above 45 degrees Celsius. Alkaloid degradation; nicotine degradation; 6-hydroxypseudooxynicotine from nicotine (R-isomer route): step 2/2. Monomer. Induced in the presence of D-nicotine (PubMed:5849820). Expressed during stationary phase (PubMed:4019415). Belongs to the oxygen-dependent FAD-linked oxidoreductase family. Extended N-terminus.