ID   FMO2_MACMU              Reviewed;         535 AA.
AC   Q28505;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 2;
DE            EC=1.14.13.8;
DE   AltName: Full=Pulmonary flavin-containing monooxygenase 2;
DE            Short=FMO 2;
DE   AltName: Full=FMO 1B1;
DE   AltName: Full=Dimethylaniline oxidase 2;
GN   Name=FMO2;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97214641; PubMed=9061021; DOI=10.1016/S0167-4781(97)00004-3;
RA   Yueh M.-F., Krueger S.K., Williams D.E.;
RT   "Pulmonary flavin-containing monooxygenase (FMO) in rhesus macaque:
RT   expression of FMO2 protein, mRNA and analysis of the cDNA.";
RL   Biochim. Biophys. Acta 1350:267-271(1997).
CC   -!- FUNCTION: This protein is involved in the oxidative metabolism of
CC       a variety of xenobiotics such as drugs and pesticides.
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   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum
CC       membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; U59453; AAB02939.1; -; mRNA.
DR   RefSeq; NP_001036242.1; -.
DR   UniGene; Mmu.3381; -.
DR   Ensembl; ENSMMUG00000019727; Macaca mulatta.
DR   GeneID; 703639; -.
DR   KEGG; mcc:703639; -.
DR   HOVERGEN; Q28505; -.
DR   BRENDA; 1.14.13.8; 1774.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
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; IPR002254; Flavin_mOase_2.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01122; FMOXYGENASE2.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Magnesium;
KW   Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW   Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    535       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 2.
FT                                /FTId=PRO_0000147647.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   535 AA;  60961 MW;  85621203B07CCFAE CRC64;
     MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKEKVEDG RASIYQSVVT
     NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS
     SSGQWKVVTQ SNGKEQSAVF DAVMVCTGHH FLPHIPLKSF PGIERFKGQY FHSRQYKHPD
     GFEGKRILVI GMGNSGSDIA VELSKSAAQV FISTRHGTWV MSRVSEDGYP WDSVFHTRFR
     SMLRNVLPRT VVKWMIEQQM NQWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK
     STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH
     LEKSTFACIG LIQPLGSIFP TAELQARWVT RVFKGLCHLP SERTMMMDII KRNEKRIDLF
     GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLFFGPCNS YQYRLAGPGQ
     WEGARSAIFT QKQRILKPLK TRVLKDSSNF PVSFLLKILG LVAVVVAFFC QLQWS
//