ID A0A3B3SAE9_9TELE Unreviewed; 523 AA.
AC A0A3B3SAE9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000027195.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000027195.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR000332, 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 AlphaFoldDB; A0A3B3SAE9; -.
DR Ensembl; ENSPKIT00000007961.1; ENSPKIP00000027195.1; ENSPKIG00000009275.1.
DR GeneTree; ENSGT00940000160836; -.
DR Proteomes; UP000261540; Unplaced.
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; 3.
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 PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF210; FLAVIN-CONTAINING MONOOXYGENASE; 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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW 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};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|PIRNR:PIRNR000332};
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}.
SQ SEQUENCE 523 AA; 59659 MW; 668BA6511B02D03B CRC64;
MACRVAVIGG GISGLICIKC CLDEGLEPVC FESSDDIGGL WRFKEEPEKD RASIYPSVTI
NTSKEMMSFS DFPIPAHFPN YMHNSLIMDY FQMYAEHFKL LRYVRFQTTV CSVSQRPDFA
RSGQWDVVTK NRQGQEERHI FDAIFVCIGH HACPHIPLKD FPGIETFKGK WFHSRDYKSP
EEWLGKRVVV IGIGNSGGDI AVELSRVAKQ VFLSTRRGAW ILNRVGENGF PMDMKLSRLT
HILTVILPIT LTSMIGERRL NKRFNHKLYS IKPKHRLLSQ HPMVNDELPN RILSGTVLVK
TNVSRIKGSS VMFEDGTVEE DIDLVVFATG YTFSFPFLPS SVISVSENKT LLYKYVFPPT
LERPTLAIIG LVQPLGAIMP ISEMQARWAT RVFKGLNKLP PVNRMLKDIK VTKEKMGKRY
VTSQRHTIQV DYVHYMDELA RQFGVRPKLL RLLLRDPRLG LSVLLGPCTP YQYRLYGPGQ
WEGARQAILT QWERVAQPMK TRAVPEPPSS RLPLLLALIL MNF
//