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 01-OCT-1996 (REL. 34, 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; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; ARTIODACTYLA. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 136-150 AND 308-317. RC TISSUE=LIVER; RX MEDLINE; 90212556. RA GASSER R., TYNES R.E., LAWTON M.P., KORSMEYER K.K., ZIEGLER D.M., RA PHILPOT R.M.; RL BIOCHEMISTRY 29:119-124(1990). RN [2] RP SEQUENCE OF 1-13 AND 184-201, AND ACETYLATION. RC TISSUE=LIVER; RX MEDLINE; 90343821. RA GUAN S.H., FALICK A.M., CASHMAN J.R.; RL BIOCHEM. BIOPHYS. RES. COMMUN. 170:937-943(1990). RN [3] RP SEQUENCE OF 185-207. RC TISSUE=LIVER; RX MEDLINE; 95278229. RA WU R.-F., ICHIKAWA Y.; RL EUR. J. BIOCHEM. 229:749-753(1995). 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 -!- SUBCELLULAR LOCATION: MICROSOMAL. CC -!- COFACTOR: FAD FLAVOPROTEIN. CC -!- TISSUE SPECIFICITY: LIVER. CC -!- SIMILARITY: STRONG, WITH OTHER MAMMALIAN FORMS OF FMO. 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; G164455; -. DR PIR; A33768; A33768. KW OXIDOREDUCTASE; MONOOXYGENASE; NADP; FLAVOPROTEIN; FAD; MICROSOME; KW TRANSMEMBRANE; MULTIGENE FAMILY; ACETYLATION. 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. SQ SEQUENCE 531 AA; 59821 MW; 22C4ADFE CRC32; 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 //