ID M3YVY3_MUSPF Unreviewed; 532 AA.
AC M3YVY3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] {ECO:0000256|PIRNR:PIRNR000332};
DE EC=1.14.13.148 {ECO:0000256|PIRNR:PIRNR000332};
DE EC=1.14.13.8 {ECO:0000256|PIRNR:PIRNR000332};
GN Name=FMO1 {ECO:0000313|Ensembl:ENSMPUP00000015493.1,
GN ECO:0000313|RefSeq:XP_004756753.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015493.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015493.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004756753.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004756753.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Broad spectrum monooxygenase that catalyzes the oxygenation
CC of a wide variety of nitrogen- and sulfur-containing compounds
CC including xenobiotics. Catalyzes the S-oxygenation of hypotaurine to
CC produce taurine, an organic osmolyte involved in cell volume regulation
CC as well as a variety of cytoprotective and developmental processes. In
CC vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce
CC trimethylamine N-oxide (TMAO) and could therefore participate to the
CC detoxification of this compound that is generated by the action of gut
CC microbiota from dietary precursors such as choline, choline containing
CC compounds, betaine or L-carnitine. {ECO:0000256|PIRNR:PIRNR000332}.
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 Evidence={ECO:0000256|ARBA:ARBA00000700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24469;
CC Evidence={ECO:0000256|ARBA:ARBA00000700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypotaurine + NADH + O2 = H2O + NAD(+) + taurine;
CC Xref=Rhea:RHEA:74111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57853,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:507393; EC=1.14.13.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74112;
CC Evidence={ECO:0000256|ARBA:ARBA00034447};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypotaurine + NADPH + O2 = H2O + NADP(+) + taurine;
CC Xref=Rhea:RHEA:69819, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57853,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:507393; EC=1.14.13.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034434};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69820;
CC Evidence={ECO:0000256|ARBA:ARBA00034434};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + O2 + trimethylamine = H2O + NADP(+) + trimethylamine
CC N-oxide; Xref=Rhea:RHEA:31979, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15724, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58389; EC=1.14.13.148;
CC Evidence={ECO:0000256|ARBA:ARBA00034415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31980;
CC Evidence={ECO:0000256|ARBA:ARBA00034415};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR000332}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177}.
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DR EMBL; AEYP01041825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004756753.1; XM_004756696.3.
DR RefSeq; XP_012913845.1; XM_013058391.1.
DR STRING; 9669.ENSMPUP00000015493; -.
DR Ensembl; ENSMPUT00000015734.1; ENSMPUP00000015493.1; ENSMPUG00000015603.1.
DR GeneID; 101682297; -.
DR KEGG; mpuf:101682297; -.
DR CTD; 2326; -.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000160945; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR OMA; VMIKEVN; -.
DR OrthoDB; 2079054at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
DR GO; GO:0042412; P:taurine biosynthetic process; IEA:Ensembl.
DR GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002253; Flavin_mOase_1.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF154; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING] 1; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01121; FMOXYGENASE1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000332};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000332};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000332};
KW Membrane {ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|PIRNR:PIRNR000332};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000332};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000332};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 532 AA; 60264 MW; 20B03CB1D8F2B0E9 CRC64;
MAKRVAIVGA GVSGLASVKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS
NSCKEMSCYS DFPFPEDYPN YVPNSQFLEY LKMYANRFNL LEYIRFKTKV CQVTKCPDFT
VTGQWEVVTQ HEGKQQSAVF DAVMVCTGFL TNPYLPLDSF PGINIFKGQY FHSRQYKHPD
IFKDKRVLVI GMGNSGTDIA VEASHLAKKV FLSTTGGAWV MSRVFDSGYP WDMVFMTRFQ
NMLRNSLPTP IVTWLMARKM NSWFNHANYG LIPEDRTQLR EPVLNDELPG RIITGKVLIK
PSIKEVKENS VIFNNTPKEE PIDIIVFATG YTFAFPFLDE TIVKVENGQA SLYKYIFPAH
LPQPTLAVIG LIKPLGSMIP TGETQARWAV RVLKGINKLP PQNVMIEEVN ERKENKHSGF
GLCYCKALQS DYITYIDELL TSINAKPNLF SLLLTDPRLA FTIFFGPCTP YQFRLTGPGK
WKGARNAILT QWDRTFKVTK TRIVQESPSP FASLLKLLSL LALLLAIFLI FL
//
