ID   A0A023GL55_AMBTT        Unreviewed;       541 AA.
AC   A0A023GL55;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-NOV-2024, entry version 41.
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   -!- FUNCTION: Acts as a Baeyer-Villiger monooxygenase on a broad range of
CC       substrates. Catalyzes the insertion of an oxygen atom into a carbon-
CC       carbon bond adjacent to a carbonyl, which converts ketones to esters.
CC       Active on diverse carbonyl compounds, whereas soft nucleophiles are
CC       mostly non- or poorly reactive. In contrast with other forms of FMO it
CC       is non- or poorly active on 'classical' substrates such as drugs,
CC       pesticides, and dietary components containing soft nucleophilic
CC       heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on
CC       an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the
CC       absence of substrates, shows slow but yet significant NADPH oxidase
CC       activity. Acts as a positive modulator of cholesterol biosynthesis as
CC       well as glucose homeostasis, promoting metabolic aging via pleiotropic
CC       effects. {ECO:0000256|ARBA:ARBA00045722}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranial + NADPH + O2 + H(+) = (1E)-2,6-
CC         dimethylhepta-1,5-dien-1-yl formate + NADP(+) + H2O;
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=octan-3-one + NADPH + O2 + H(+) = pentyl propanoate + NADP(+)
CC         + H2O; Xref=Rhea:RHEA:54840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         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=octan-3-one + NADPH + O2 + H(+) = ethyl hexanoate + NADP(+) +
CC         H2O; 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=sulcatone + NADPH + O2 + H(+) = 4-methylpent-3-en-1-yl acetate
CC         + NADP(+) + H2O; 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=NADPH + O2 + H(+) = 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=heptan-2-one + NADPH + O2 + H(+) = pentyl acetate + NADP(+) +
CC         H2O; 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=heptan-4-one + NADPH + O2 + H(+) = propyl butanoate + NADP(+)
CC         + H2O; Xref=Rhea:RHEA:54852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         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=hexan-3-one + NADPH + O2 + H(+) = propyl propanoate + NADP(+)
CC         + H2O; Xref=Rhea:RHEA:54848, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         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=hexan-3-one + NADPH + O2 + H(+) = ethyl butanoate + NADP(+) +
CC         H2O; 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|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; 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   FunFam; 3.50.50.60:FF:000159; Dimethylaniline monooxygenase [N-oxide-forming]; 1.
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
//