ID   FMO5_CAVPO              Reviewed;         533 AA.
AC   P49109;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 55.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 5;
DE            EC=1.14.13.8;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 5;
DE            Short=FMO 5;
DE   AltName: Full=Dimethylaniline oxidase 5;
GN   Name=FMO5;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley; TISSUE=Liver;
RX   MEDLINE=95177663; PubMed=7872795; DOI=10.1006/abbi.1995.1163;
RA   Overby L.H., Buckpitt A.R., Lawton M.P., Atta-Asafo-Adjei E.,
RA   Schulze J., Philpot R.M.;
RT   "Characterization of flavin-containing monooxygenase 5 (FMO5) cloned
RT   from human and guinea pig: evidence that the unique catalytic
RT   properties of FMO5 are not confined to the rabbit ortholog.";
RL   Arch. Biochem. Biophys. 317:275-284(1995).
CC   -!- FUNCTION: In contrast with other forms of FMO it does not seem to
CC       be a drug-metabolizing enzyme.
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   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; L37081; AAA67848.1; -; mRNA.
DR   PIR; S71617; S71617.
DR   HOVERGEN; P49109; -.
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:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004499; F:flavin-containing monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012143; dManiline_mOase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR002257; Flavin_mOase_5.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01125; FMOXYGENASE5.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
KW   Methylation; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW   Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    533       Dimethylaniline monooxygenase [N-oxide-
FT                                forming] 5.
FT                                /FTId=PRO_0000147664.
FT   NP_BIND      10     15       FAD (Potential).
FT   NP_BIND     192    197       NADP (By similarity).
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
FT   MOD_RES       5      5       Omega-N-methylated arginine (By
FT                                similarity).
SQ   SEQUENCE   533 AA;  60125 MW;  E0C06EE4C6B6EFDD CRC64;
     MTKKRIAVIG GGVSGLSSIK CCLEEGLEPV CFERSADIGG LWRFQENPEE GRASIYKSVI
     INTSKEMMCF SDYPIPDHYP NFMHNSHVLE YFRMYAKEFG LLKYIQFKTT VCNVKKRPDF
     STSGQWEVVT EHEGKTKVDV FDAVMVCTGH HTNAHLPLES FPGIEKFKGQ YFHSRDYKNP
     EAFTGKRVVI IGIGNSGGDL AVEISHTAKQ VFLSTRRGSW ILNRVGKHGY PTDVLLSSRF
     TYFLSKILGQ SLSNAYVEKQ MNERFDHEMF GLKPKHRAMS QHPTVNDDLP NRIIAGMVKV
     KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFDFPFLE DSVKVVKNKV SLYKKVFPPN
     LERPTLAIIG LIQPLGAIMP ISELQGRWAV QVFKGLKTLP SQSEMMAEIT KAQEEIAKRY
     VDSQRHTIQG DYIQTMEEIA EFVGVKPNLL SLAFTDPKLA LKLFFGPCTP IHYRLQGPGK
     WHGARKAILT TYDRIRKPLN TRETEKSNSM VSAVTTGCFM LAVVFFAIIM AYA
//