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Database: UniProt
Entry: Q3SZW0_BOVIN
LinkDB: Q3SZW0_BOVIN
Original site: Q3SZW0_BOVIN 
ID   Q3SZW0_BOVIN            Unreviewed;       429 AA.
AC   Q3SZW0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   Name=FMO3 {ECO:0000313|EMBL:AAI02684.1,
GN   ECO:0000313|Ensembl:ENSBTAP00000027198.2,
GN   ECO:0000313|VGNC:VGNC:29051};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI02684.1};
RN   [1] {ECO:0000313|EMBL:AAI02684.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hereford {ECO:0000313|EMBL:AAI02684.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:AAI02684.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000027198.2, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027198.2,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSBTAP00000027198.2}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027198.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-nicotine + NADPH + O2 = H2O + NADP(+) + trans-(S)-nicotine
CC         N(1')-oxide; Xref=Rhea:RHEA:58720, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:59806, ChEBI:CHEBI:142660;
CC         Evidence={ECO:0000256|ARBA:ARBA00036085};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58721;
CC         Evidence={ECO:0000256|ARBA:ARBA00036085};
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 + 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=albendazole + H(+) + NADPH + O2 = albendazole S-oxide + H2O +
CC         NADP(+); Xref=Rhea:RHEA:10796, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16664, ChEBI:CHEBI:16959,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.32;
CC         Evidence={ECO:0000256|ARBA:ARBA00036808};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10797;
CC         Evidence={ECO:0000256|ARBA:ARBA00036808};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361177};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004111}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004111}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC       ECO:0000256|RuleBase:RU361177}.
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DR   EMBL; BC102683; AAI02684.1; -; mRNA.
DR   Ensembl; ENSBTAT00000027198.3; ENSBTAP00000027198.2; ENSBTAG00000020597.6.
DR   VEuPathDB; HostDB:ENSBTAG00000020597; -.
DR   VGNC; VGNC:29051; FMO3.
DR   GeneTree; ENSGT00940000161339; -.
DR   HOGENOM; CLU_006909_8_0_1; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000020597; Expressed in metanephros cortex and 69 other cell types or tissues.
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-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR002255; Flavin_mOase_3.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF44; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING] 3; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01123; FMOXYGENASE3.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361177}; Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU361177}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361177};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q3SZW0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
SQ   SEQUENCE   429 AA;  48534 MW;  3CD2DAE8D91F466D CRC64;
     MVKKVAIIGA GISGLASIRN CLEEGLEPTC FEKGEDIGGL WKFSDHVEEG RASIYRSVFT
     NSSKEMTCFP DFPFPDDFPN FMHNSKLQEY ITMFAKEKNL LKYIQFKTIV SSVNKRPDFQ
     TTGQWDVITE KDGKKESAVF DAVMICSGHH VYPNIPKESF PGIKLFKGKC FHSRDYKEPG
     IFKGKRVLVI GLGNSGCDIA SELSHIAEKV IISSRSGSWV MSRVWDEGYP WDMLFITRFE
     TFLKNTLPTV ISNWWYMKQM NARFKHENYG LMPLNSTLRK EPVFNDELPA CILCGIVTIK
     PNVKEFTEDS AIFEDGTVFK AIDYVIFATG YSYAYPFLDD SIIKSRDNEV TLFKGIFPPP
     LEKPTLAVIG LVQSLGAAIP TTDLQSRWAV QVIKGTCPLP SVKDMMNDID EKMGKKLKLQ
     FLLFPGQDK
//
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