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; MAMMALIA; EUTHERIA; OC ARTIODACTYLA; SUIFORMES; SUINA; SUIDAE; SUS. 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.; 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. 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. 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). 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 FLAVOPROTEIN. CC -!- SUBCELLULAR LOCATION: MICROSOMAL. CC -!- TISSUE SPECIFICITY: LIVER. CC -!- SIMILARITY: BELONGS TO THE FMO FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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. DR PFAM; PF00743; FMO-like; 1. 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 //