FMO1_CAVPO
ID FMO1_CAVPO Reviewed; 19 AA.
AC P49328;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
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;
DE Flags: Fragment;
GN Name=FMO1; Synonyms=FMO-1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2369122; DOI=10.1016/0003-9861(90)90334-u;
RA Yamada H., Yuno K., Oguri K., Yoshimura H.;
RT "Multiplicity of liver microsomal flavin-containing monooxygenase in the
RT guinea pig: its purification and characterization.";
RL Arch. Biochem. Biophys. 280:305-312(1990).
CC -!- FUNCTION: This protein is involved in the oxidative metabolism of a
CC variety of xenobiotics such as drugs and pesticides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-
CC dimethylaniline N-oxide + NADP(+); Xref=Rhea:RHEA:24468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16269, ChEBI:CHEBI:17735, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.8;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR PIR; S10747; S10747.
DR AlphaFoldDB; P49328; -.
DR eggNOG; KOG1399; Eukaryota.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein;
KW Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane.
FT CHAIN 1..>19
FT /note="Dimethylaniline monooxygenase [N-oxide-forming] 1"
FT /id="PRO_0000147638"
FT BINDING 8..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT NON_TER 19
SQ SEQUENCE 19 AA; 1826 MW; 324DDEB75CA05522 CRC64;
VKKVAIIGAG VSGLASIRS