ID FMO1_PIG STANDARD; PRT; 531 AA. AC P16549; DT 01-AUG-1990 (Rel. 15, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Dimethylaniline monooxygenase [N-oxide forming] 1 (EC 1.14.13.8) DE (Hepatic flavin-containing monooxygenase 1) (FMO 1) (Dimethylaniline DE oxidase 1). GN FMO1 OR FMO-1. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 136-150 AND 308-317. RC TISSUE=Liver; RX MEDLINE=90212556; PubMed=2322534; 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 SEQUENCE OF 1-13 AND 184-201, AND ACETYLATION. RC TISSUE=Liver; RX MEDLINE=90343821; PubMed=2383273; 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 SEQUENCE OF 185-207. RC TISSUE=Liver; RX MEDLINE=95278229; PubMed=7758472; 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 CARBOHYDRATE-LINKAGE SITE. RX MEDLINE=98451545; PubMed=9778310; 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) = CC N,N-DIMETHYLANILINE N-OXIDE + NADP(+) + H(2)O. CC -!- COFACTOR: FAD. CC -!- SUBCELLULAR LOCATION: MICROSOMAL. 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; -. DR PIR; A33768; A33768. DR InterPro; IPR000960; FMO. DR Pfam; PF00743; FMO-like; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01121; FMOXYGENASE1. KW Oxidoreductase; Monooxygenase; NADP; Flavoprotein; FAD; Microsome; KW Transmembrane; Multigene family; Acetylation; Glycoprotein. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT NP_BIND 8 13 FAD (ADP PART) (POTENTIAL). FT NP_BIND 190 195 NADP (POTENTIAL). FT ACT_SITE 207 207 SUBSTRATE-BINDING. FT CARBOHYD 119 119 N-LINKED (GLCNAC...) (HIGH MANNOSE). SQ SEQUENCE 531 AA; 59821 MW; 5E475E6BD81C8157 CRC64; AKRVAIVGAG VSGLASIKCC LEEGLEPTCF ERSDDLGGLW RFTEHVEEGR ASLYKSVVSN SCKEMSCYPD FPFPEDYPNY VPNSHFLEYL RMYANQFNLL KCIQFKTKVC SVTKHEDFNT TGQWDVVTLC EGKQESAVFD AVMVCTGFLT NPYLPLDSFP GINTFKGQYF HSRQYKHPDI FKDKSVLVVG MGNSGTDIAV EASHLAKKVF LSTTGGAWVI SRVFDSGYPW DMVFMTRFQN MFRNSLPTPI VNWLIAKKMN SWFNHANYGL IPEDRIQLRE PVLNDELPGR IITGKVLIKP SIKEVKENSV VFNSSPEEEP IDIIVFATGY TFAFPFLDES VVKVEDGQAS LYKYIFPAHL QKPTLAVIGL IKPLGSLLPT GDTQARWAVR VLKGVNKLPP SSVMIQEVNT RKENKPSGFG LCYCKALQSD YIAYIDELLT YIDAKPNMFS LLLTDPHLAL TIFFGPCTPY QFRLTGPGKW EGARNAIMTQ WDRTFKVTKT RIVKESPSPF ASLLKLFSFL ALLVAIFQIF L //