ID   A0A023GL55_AMBTT        Unreviewed;       541 AA.
AC   A0A023GL55;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JUL-2024, entry version 40.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
OS   Amblyomma triste (Neotropical tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae; Amblyomma.
OX   NCBI_TaxID=251400 {ECO:0000313|EMBL:JAC34616.1};
RN   [1] {ECO:0000313|EMBL:JAC34616.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mato Grasso do Sul {ECO:0000313|EMBL:JAC34616.1};
RC   TISSUE=Salivary glands {ECO:0000313|EMBL:JAC34616.1};
RA   Garcia G.R., Gardinassi L.G., Ribeiro J.M., Anatriello E., Ferreira B.R.,
RA   Moreira H.N., Mafra C., Olegario M.M., Szabo P.J., Miranda-Santos I.K.,
RA   Maruyama S.R.;
RT   "The sialotranscriptome of Amblyomma triste, Amblyomma parvum and Amblyomma
RT   cajennense ticks, uncovered by 454-based RNA-seq.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-
CC         dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+);
CC         Xref=Rhea:RHEA:54860, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16980, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:138375;
CC         Evidence={ECO:0000256|ARBA:ARBA00023916};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54861;
CC         Evidence={ECO:0000256|ARBA:ARBA00023916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + octan-3-one = H2O + NADP(+) + pentyl
CC         propanoate; Xref=Rhea:RHEA:54840, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:80946, ChEBI:CHEBI:87373;
CC         Evidence={ECO:0000256|ARBA:ARBA00001029};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54841;
CC         Evidence={ECO:0000256|ARBA:ARBA00001029};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + octan-3-one = ethyl hexanoate + H2O +
CC         NADP(+); Xref=Rhea:RHEA:54856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:80946, ChEBI:CHEBI:86055;
CC         Evidence={ECO:0000256|ARBA:ARBA00001105};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54857;
CC         Evidence={ECO:0000256|ARBA:ARBA00001105};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + sulcatone = 4-methylpent-3-en-1-yl acetate
CC         + H2O + NADP(+); Xref=Rhea:RHEA:54864, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16310,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138373;
CC         Evidence={ECO:0000256|ARBA:ARBA00000299};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54865;
CC         Evidence={ECO:0000256|ARBA:ARBA00000299};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000458};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11261;
CC         Evidence={ECO:0000256|ARBA:ARBA00000458};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + heptan-2-one + NADPH + O2 = H2O + NADP(+) + pentyl
CC         acetate; Xref=Rhea:RHEA:54836, ChEBI:CHEBI:5672, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:87362;
CC         Evidence={ECO:0000256|ARBA:ARBA00000019};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54837;
CC         Evidence={ECO:0000256|ARBA:ARBA00000019};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + heptan-4-one + NADPH + O2 = H2O + NADP(+) + propyl
CC         butanoate; Xref=Rhea:RHEA:54852, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:89484, ChEBI:CHEBI:89719;
CC         Evidence={ECO:0000256|ARBA:ARBA00001839};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54853;
CC         Evidence={ECO:0000256|ARBA:ARBA00001839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexan-3-one + NADPH + O2 = H2O + NADP(+) + propyl
CC         propanoate; Xref=Rhea:RHEA:54848, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:89828, ChEBI:CHEBI:89891;
CC         Evidence={ECO:0000256|ARBA:ARBA00000279};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54849;
CC         Evidence={ECO:0000256|ARBA:ARBA00000279};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexan-3-one + NADPH + O2 = ethyl butanoate + H2O +
CC         NADP(+); Xref=Rhea:RHEA:54844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:88764, ChEBI:CHEBI:89891;
CC         Evidence={ECO:0000256|ARBA:ARBA00000531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54845;
CC         Evidence={ECO:0000256|ARBA:ARBA00000531};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000332,
CC         ECO:0000256|RuleBase:RU361177};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004586, ECO:0000256|PIRNR:PIRNR000332}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004524}.
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; GBBM01000802; JAC34616.1; -; mRNA.
DR   AlphaFoldDB; A0A023GL55; -.
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:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR002257; Flavin_mOase_5.
DR   InterPro; IPR050346; FMO.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF166; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING]; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01125; FMOXYGENASE5.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {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   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Monooxygenase {ECO:0000256|PIRNR:PIRNR000332,
KW   ECO:0000256|RuleBase:RU361177};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000332};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000332};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   541 AA;  61544 MW;  165500E50F7EA1D2 CRC64;
     MSEARGRVCV VGAGSSGLTT ARQMLDYGFD VVLYERSGDV GGLWAYHDDD VEGQASVMRT
     TIINTSKEMS AFSDFPPPKD LPNYMHNTKM LGYFRSYADH FGVTKYVKTR HDVVQVTPAA
     DYDKTGRWDV VVRDLETNTD RTETFEAVAV CVGHHVYPNV PSFKGQEKFR GRVLHTHSLK
     NADKFRDHRV AVVGIGNSAV DAVVDVSHVA IETYLSTRRG AWVAKRVGPN GMPIDIFLST
     RLKNYLMHML PESVSNDYVE NILNGFFNHE VYGIKPKHRY NAQHPTVNDA LPNLILSGKV
     QVKKNVVEFT EEGVLFEGDN KVTQLDDVIL ATGYQIKFPF LPKDVVSVVD NQVQLYKYVF
     PPHLKHPTMA IIGLIQPIGA IFPIAELQAR WMAELLTKKR SLPSEEAMHE NIRKKLAAMR
     RRYVDSPRHT IQVDWIDYMD ELASQIGARP NMIKYLLTDY ELFRALLGPC VPYQFRLEGP
     HRWPGARQAI LDSRSRVMYP LNDRCSSFRR KDKGHFTFFN VCAFFFVLAV AYIFSGLRQH
     S
//