ID   FMO1_CANLF              Reviewed;         532 AA.
AC   Q95LA2;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1;
DE            EC=1.14.13.8;
DE   AltName: Full=Dimethylaniline oxidase 1;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 1;
DE            Short=FMO 1;
GN   Name=FMO1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=11792679; DOI=10.1124/dmd.30.2.119;
RA   Lattard V., Longin-Sauvageon C., Lachuer J., Delatour P., Benoit E.;
RT   "Cloning, sequencing, and tissue-dependent expression of flavin-containing
RT   monooxygenase (FMO) 1 and FMO3 in the dog.";
RL   Drug Metab. Dispos. 30:119-128(2002).
CC   -!- FUNCTION: This protein is involved in the oxidative metabolism of a
CC       variety of xenobiotics such as drugs and pesticides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-
CC         dimethylaniline N-oxide + NADP(+); Xref=Rhea:RHEA:24468,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16269, ChEBI:CHEBI:17735, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.13.8;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:11792679};
CC       Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC       membrane {ECO:0000305|PubMed:11792679}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:11792679}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; AF384053; AAK97433.1; -; mRNA.
DR   RefSeq; NP_001003061.1; NM_001003061.1.
DR   RefSeq; XP_005622281.1; XM_005622224.2.
DR   AlphaFoldDB; Q95LA2; -.
DR   SMR; Q95LA2; -.
DR   STRING; 9615.ENSCAFP00000022051; -.
DR   PaxDb; Q95LA2; -.
DR   Ensembl; ENSCAFT00030000380; ENSCAFP00030000331; ENSCAFG00030000236.
DR   Ensembl; ENSCAFT00040028004; ENSCAFP00040024320; ENSCAFG00040015175.
DR   Ensembl; ENSCAFT00845002360; ENSCAFP00845001876; ENSCAFG00845001369.
DR   GeneID; 403604; -.
DR   KEGG; cfa:403604; -.
DR   CTD; 2326; -.
DR   VEuPathDB; HostDB:ENSCAFG00845001369; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   GeneTree; ENSGT00940000160945; -.
DR   HOGENOM; CLU_006909_8_2_1; -.
DR   InParanoid; Q95LA2; -.
DR   OMA; VMIKEVN; -.
DR   OrthoDB; 405736at2759; -.
DR   TreeFam; TF105285; -.
DR   Reactome; R-CFA-217271; FMO oxidises nucleophiles.
DR   Proteomes; UP000002254; Chromosome 7.
DR   Bgee; ENSCAFG00000014982; Expressed in liver and 16 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl.
DR   GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR   Gene3D; 3.50.50.60; -; 4.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR002253; Flavin_mOase_1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01121; FMOXYGENASE1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P16549"
FT   CHAIN           2..532
FT                   /note="Dimethylaniline monooxygenase [N-oxide-forming] 1"
FT                   /id="PRO_0000147637"
FT   TRANSMEM        511..531
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         9..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         32
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         40..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         60..61
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         61..62
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         195..198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   SITE            208
FT                   /note="Important for substrate binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P16549"
SQ   SEQUENCE   532 AA;  60059 MW;  9F34585CB267592F CRC64;
     MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS
     NSCKEMSCYS DFPFPEDYPN YVPNSQFLEY LKMYANRFSL LKCIRFKTKV CKVTKCPDFT
     VTGQWEVVTQ HEGKQESAIF DAVMVCTGFL TNPHLPLDCF PGINTFKGQY FHSRQYKHPD
     IFKDKRVLVI GMGNSGTDIA VETSRLAKKV FLSTTGGAWV MSRVFDSGYP WDMVFMTRFQ
     NMFRNSLPTP IVTWLMARKM NSWFNHANYG LVPEDRTQLR EPVLNDELPG CIITGKVLIK
     PSIKEVKENS VVFNNTPKEE PIDIIVFATG YTFAFPFLDE TVVKVENGQA SLYKYIFPVH
     LPKPTLAVIG LIKPLGSMIP TGETQARWAV RVLKGINKLP PQSAMTEEVN ARKENKPSGF
     GLCYCKALQS DYITYIDELL TNINAKPNLF SLLLTDPRLA LTIFFGPCTP YQFRLTGPGK
     WKGARNAILT QWDRTFKVTK TRIVQESPTP FASLLKLLSL LALLMAIFLI FL