ID   FMO3_BOVIN              Reviewed;         532 AA.
AC   Q8HYJ9;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3;
DE            EC=1.14.13.8;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 3;
DE            Short=FMO 3;
DE   AltName: Full=Dimethylaniline oxidase 3;
GN   Name=FMO3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISEASE.
RX   MEDLINE=22354151; PubMed=12466292; DOI=10.1101/gr.240202;
RA   Lunden A., Marklund S., Gustafsson V., Andersson L.;
RT   "A nonsense mutation in the FMO3 gene underlies fishy off-flavor in
RT   cow's milk.";
RL   Genome Res. 12:1885-1888(2002).
CC   -!- FUNCTION: Involved in the oxidative metabolism of a variety of
CC       xenobiotics such as drugs and pesticides. It N-oxygenates primary
CC       aliphatic alkylamines as well as secondary and tertiary amines.
CC       Acts on TMA to produce TMA-N-oxide.
CC   -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N-
CC       dimethylaniline N-oxide + NADP(+) + H(2)O.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Microsome membrane (By similarity).
CC       Endoplasmic reticulum membrane (By similarity).
CC   -!- DISEASE: Defects in FMO3 are the cause of a fishy off-flavor in
CC       cow milk due to by an elevated level of trimethylamine (TMA) in
CC       body fluids.
CC   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; AF488422; AAN27919.1; -; mRNA.
DR   IPI; IPI00695492; -.
DR   RefSeq; NP_776482.1; -.
DR   UniGene; Bt.12519; -.
DR   Ensembl; ENSBTAG00000020597; Bos taurus.
DR   GeneID; 281167; -.
DR   KEGG; bta:281167; -.
DR   HOVERGEN; Q8HYJ9; -.
DR   BRENDA; 1.14.13.8; 251.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031227; C:intrinsic to endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004499; F:flavin-containing monooxygenase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012143; dManiline_mOase.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR002255; Flavin_mOase_3.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01123; FMOXYGENASE3.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; Transmembrane.
FT   CHAIN         1    532       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 3.
FT                                /FTId=PRO_0000147652.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (Potential).
FT   MOD_RES     401    401       Phosphoserine (By similarity).
SQ   SEQUENCE   532 AA;  60093 MW;  2CA5964889490CBA CRC64;
     MVKKVAIIGA GISGLASIRN CLEEGLEPTC FEKGEDIGGL WKFSDHVEEG RASIYRSVFT
     NSSKEMTCFP DFPFPDDFPN FMHNSKLQEY ITMFAKEKNL LKYIQFKTIV SSVNKRPDFQ
     TTGQWDVITE KDGKKESAVF DAVMICSGHH VYPNIPKESF PGIKLFKGKC FHSRDYKEPG
     IFKGKRVLVI GLGNSGCDIA SELSHIAEKV IISSRSGSWV MSRVWDEGYP WDMLFITRFE
     TFLKNTLPTV ISNWWYMKQM NARFKHENYG LMPLNSTLRK EPVFNDELPA CILCGIVTIK
     PNVKEFTEDS AIFEDGTVFK AIDYVIFATG YSYAYPFLDD SIIKSRDNEV TLFKGIFPPP
     LEKPTLAVIG LVQSLGAAIP TTDLQSRWAV QVIKGTCPLP SVKDMMNDID EKMGKKLKLF
     GKSDTIQTDY VVYMDELASF IGAKPNIPWL FLTDPKLALE VYFGPCTPYQ FRLVGPGKWP
     GARNAILTQW DRLLKPMTTR VVGSPLKPCL FCNWFRPVLI SVVSIAALIV LF
//