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}. 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 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 //