ID A0A2K5DNS9_AOTNA Unreviewed; 532 AA.
AC A0A2K5DNS9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:ENSANAP00000022629.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000022629.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000022629.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_012300130.1; XM_012444707.1.
DR STRING; 37293.ENSANAP00000022623; -.
DR Ensembl; ENSANAT00000040521.1; ENSANAP00000022623.1; ENSANAG00000029043.1.
DR Ensembl; ENSANAT00000040527.1; ENSANAP00000022629.1; ENSANAG00000029043.1.
DR GeneID; 105711798; -.
DR CTD; 2326; -.
DR GeneTree; ENSGT00940000160945; -.
DR OMA; VMIKEVN; -.
DR OrthoDB; 2079054at2759; -.
DR Proteomes; UP000233020; 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:0070995; P:NADPH oxidation; IEA:Ensembl.
DR GO; GO:0042412; P:taurine biosynthetic process; IEA:Ensembl.
DR GO; GO:0009404; P:toxin 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|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000332};
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:UP000233020};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 513..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 532 AA; 60157 MW; 748D9BF23D71812E CRC64;
MGKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYESVVS
NSCKEMSCYS DFPFPEDYPN YVPNSQFLEY LKMYANHFNL LKHIQFKTKV CSVAKCSDFT
VSGQWEVVTL HKEKQESAIF DAVMVCTGFL TNPYLPLDSF PGINAFKGQY FHSRQYKHPD
IFKDKRVLVI GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRIFDSGYP WDMVFTTRFQ
NMLRNSLPTP IVTWLMARKI NNWLNHANYG LMPDDRTQLK EFVLNDELPG RIITGKVFIR
PSIKEVKENS VIFNNTSKEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH
LQKSTLAIIG LIKPLGSMIP TGETQARWAV RVLKGVNKLP SPSVMIEEVN ARKENKPGWF
GLCYCKALQA DYITYIDELL TCINAKPNLF SMLLTDPHLA LTIFFGPCSP YQFRLTGPGK
WEGARNAIMT QWDRTFKVTK ARIVQESPSP FESFLKLFSF LALLVAIFLI FL
//
