ID A0A087QQH5_APTFO Unreviewed; 496 AA.
AC A0A087QQH5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Flavin-containing monooxygenase 3 {ECO:0000256|ARBA:ARBA00040499};
DE EC=1.14.13.148 {ECO:0000256|ARBA:ARBA00034528};
DE EC=1.14.13.32 {ECO:0000256|ARBA:ARBA00039128};
DE EC=1.14.13.8 {ECO:0000256|ARBA:ARBA00012850};
DE AltName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3 {ECO:0000256|ARBA:ARBA00043212};
DE AltName: Full=Trimethylamine monooxygenase {ECO:0000256|ARBA:ARBA00034554};
DE Flags: Fragment;
GN ORFNames=AS27_15746 {ECO:0000313|EMBL:KFM03479.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM03479.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM03479.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM03479.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; KL225810; KFM03479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QQH5; -.
DR STRING; 9233.A0A087QQH5; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
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; 1.
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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:KFM03479.1};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT NON_TER 496
FT /evidence="ECO:0000313|EMBL:KFM03479.1"
SQ SEQUENCE 496 AA; 56390 MW; 1A37852351973BA5 CRC64;
MVRRVAVVGA GVSGLAATKC CLEEGLEPIC FEQSEDVGGL WRYTDQAEEG RASIYRTVFT
NSCKEMMCYP DFPFPDDHPN YMHNARVQHY ICKYAEHFDL LRHVQFKTLV TKVKKRPDFS
VTGQWEVVTQ RDGKEETAVF DAVMVCSGHH VYPNLPLADF PGIQKFKGCY FHSREYKEPE
KFRGKKVLVV GLGNSGCDIA VELSTVASQV YLSSRSGSWV MSRVWDNGYP WDMLVITRFR
TWLGNILPRA LSDWLYVRGM NRFFKHENFG LMPLNRTSRK EPVFNDDLPS RIACGVVVMK
PNVKEFRETS VLFQDGTVQD DVDAVVFATG YSYSYPFMED DSIIKSRDNQ VTLYKGILPP
LLEKPTMAVI GLVQSLGPII PTVDLQCRWA VKVFQGQCML PPVSEMIDDV DEKMGKKLKW
YGSSTTLQTD YIAYMDELAS AIGVKPNVLK LLLTDPWLAL EVIFGPCSPY QFRLMGPGKW
NGARKAILTQ WDRTLQ
//
