ID   FMO2_PONAB              Reviewed;         535 AA.
AC   Q5REK0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 33.
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   Pongo abelii (Sumatran orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is involved in the oxidative metabolism of
CC       a variety of xenobiotics such as drugs and pesticides (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N-
CC       dimethylaniline N-oxide + NADP(+) + H(2)O.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane (By similarity).
CC       Endoplasmic reticulum membrane (By similarity).
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DR   EMBL; CR857525; CAH89807.1; -; mRNA.
DR   RefSeq; NP_001124835.1; -.
DR   UniGene; Pab.19417; -.
DR   GeneID; 100171693; -.
DR   HOVERGEN; Q5REK0; -.
DR   BRENDA; 1.14.13.8; 269192.
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_0000229039.
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;  60978 MW;  16FCCC733693E13D CRC64;
     MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG RASIYQSVVT
     NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS
     SSGQWKVVTQ SNSKEQSAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPD
     GFEGKRILVI GMGNSGSDIA VELSKNAAQV FISTRHGTWV LSRISEDGYP WDSVFHTRFR
     SMLRRVLPRT AVKWMIEQQM NRWFNHENYG LEPQNKYFMK EPVLNDDVPS RLLCGAIKVK
     STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH
     LEKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP SERTMMMDII KRNEKRIELF
     GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLYFGPCNS YQYRLVGPGQ
     WEGARSAIFT QKQRILKPLK TRALKDSSNF SVSFLLKILG LLAVVVAFFC QLQWS
//