ID FMO1_PIG Reviewed; 532 AA. AC P16549; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-NOV-2010, entry version 93. 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; Synonyms=FMO-1; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 137-151 AND RP 309-318. RC TISSUE=Liver; RX MEDLINE=90212556; PubMed=2322534; DOI=10.1021/bi00453a014; RA Gasser R., Tynes R.E., Lawton M.P., Korsmeyer K.K., Ziegler D.M., RA Philpot R.M.; RT "The flavin-containing monooxygenase expressed in pig liver: primary RT sequence, distribution, and evidence for a single gene."; RL Biochemistry 29:119-124(1990). RN [2] RP PROTEIN SEQUENCE OF 2-14 AND 185-202, AND ACETYLATION AT ALA-2. RC TISSUE=Liver; RX MEDLINE=90343821; PubMed=2383273; DOI=10.1016/0006-291X(90)92181-X; RA Guan S.H., Falick A.M., Cashman J.R.; RT "N-terminus determination: FAD and NADP binding domain mapping of hog RT liver flavin-containing monooxygenase by tandem mass spectrometry."; RL Biochem. Biophys. Res. Commun. 170:937-943(1990). RN [3] RP PROTEIN SEQUENCE OF 186-208. RC TISSUE=Liver; RX MEDLINE=95278229; PubMed=7758472; RX DOI=10.1111/j.1432-1033.1995.tb20523.x; RA Wu R.-F., Ichikawa Y.; RT "An essential lysyl residue (Lys208) in the substrate-binding site of RT porcine FAD-containing monooxygenase."; RL Eur. J. Biochem. 229:749-753(1995). RN [4] RP GLYCOSYLATION AT ASN-120. RX MEDLINE=98451545; PubMed=9778310; DOI=10.1021/tx980117p; RA Korsmeyer K.K., Guan S., Yang Z.C., Falick A.M., Ziegler D.M., RA Cashman J.R.; RT "N-glycosylation of pig flavin-containing monooxygenase form 1: RT determination of the site of protein modification by mass RT spectrometry."; RL Chem. Res. Toxicol. 11:1145-1153(1998). 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. CC -!- SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum CC membrane. CC -!- TISSUE SPECIFICITY: Liver. CC -!- SIMILARITY: Belongs to the FMO family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M32031; AAA31033.1; -; mRNA. DR PIR; A33768; A33768. DR RefSeq; NP_999229.1; -. DR UniGene; Ssc.229; -. DR ProteinModelPortal; P16549; -. DR SMR; P16549; 3-442. DR Ensembl; ENSSSCT00000016637; ENSSSCP00000016191; ENSSSCG00000015268. DR GeneID; 397132; -. DR KEGG; ssc:397132; -. DR CTD; 397132; -. DR HOVERGEN; HBG002037; -. DR OMA; MLLTDPR; -. DR BRENDA; 1.14.13.8; 249. 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; IDA:BHF-UCL. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0070995; P:NADPH oxidation; IDA:BHF-UCL. DR GO; GO:0006082; P:organic acid metabolic process; IDA:BHF-UCL. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009404; P:toxin metabolic process; IDA:BHF-UCL. DR InterPro; IPR012143; dManiline_mOase. DR InterPro; IPR000960; Flavin_mOase. DR InterPro; IPR020946; Flavin_mOase-like. DR InterPro; IPR002253; Flavin_mOase_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2. DR Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01121; FMOXYGENASE1. PE 1: Evidence at protein level; KW Acetylation; Direct protein sequencing; Endoplasmic reticulum; FAD; KW Flavoprotein; Glycoprotein; Membrane; Microsome; Monooxygenase; NADP; KW Oxidoreductase; Transmembrane. FT INIT_MET 1 1 Removed. FT CHAIN 2 532 Dimethylaniline monooxygenase [N-oxide- FT forming] 1. FT /FTId=PRO_0000147641. FT NP_BIND 9 14 FAD (Potential). FT NP_BIND 191 196 NADP (Potential). FT SITE 208 208 Important for substrate binding. FT MOD_RES 2 2 N-acetylalanine. FT CARBOHYD 120 120 N-linked (GlcNAc...) (high mannose). SQ SEQUENCE 532 AA; 59952 MW; 5E475E7F2F3B8A67 CRC64; MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS NSCKEMSCYP DFPFPEDYPN YVPNSHFLEY LRMYANQFNL LKCIQFKTKV CSVTKHEDFN TTGQWDVVTL CEGKQESAVF DAVMVCTGFL TNPYLPLDSF PGINTFKGQY FHSRQYKHPD IFKDKSVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMVFMTRFQ NMFRNSLPTP IVNWLIAKKM NSWFNHANYG LIPEDRIQLR EPVLNDELPG RIITGKVLIK PSIKEVKENS VVFNSSPEEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH LQKPTLAVIG LIKPLGSLLP TGDTQARWAV RVLKGVNKLP PSSVMIQEVN TRKENKPSGF GLCYCKALQS DYIAYIDELL TYIDAKPNMF SLLLTDPHLA LTIFFGPCTP YQFRLTGPGK WEGARNAIMT QWDRTFKVTK TRIVKESPSP FASLLKLFSF LALLVAIFQI FL //