ID A0A023GL55_AMBTT Unreviewed; 541 AA. AC A0A023GL55; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 29-SEP-2021, entry version 32. DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] {ECO:0000256|PIRNR:PIRNR000332}; DE EC=1.14.13.8 {ECO:0000256|PIRNR:PIRNR000332}; 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(+) + 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|PIRNR:PIRNR000332}; 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|PIRNR:PIRNR000332}. CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183, CC ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GBBM01000802; JAC34616.1; -; mRNA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. 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 Gene3D; 3.50.50.60; -; 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 Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01125; FMOXYGENASE5. DR SUPFAM; SSF51905; SSF51905; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000332}; KW Methylation {ECO:0000256|ARBA:ARBA00022481}; KW Microsome {ECO:0000256|PIRNR:PIRNR000332}; 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 //