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Database: UniProt
Entry: A0A2K5C6N6_AOTNA
LinkDB: A0A2K5C6N6_AOTNA
Original site: A0A2K5C6N6_AOTNA 
ID   A0A2K5C6N6_AOTNA        Unreviewed;       533 AA.
AC   A0A2K5C6N6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Flavin-containing monooxygenase 5 {ECO:0000256|PIRNR:PIRNR000332};
DE            EC=1.14.13.8 {ECO:0000256|PIRNR:PIRNR000332};
DE            EC=1.6.3.1 {ECO:0000256|PIRNR:PIRNR000332};
GN   Name=FMO5 {ECO:0000313|Ensembl:ENSANAP00000004361.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000004361.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000004361.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Acts as 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       {ECO:0000256|PIRNR:PIRNR000332}.
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|ARBA:ARBA00000700};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24469;
CC         Evidence={ECO:0000256|ARBA:ARBA00000700};
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   RefSeq; XP_012327405.1; XM_012471982.1.
DR   RefSeq; XP_012327406.1; XM_012471983.1.
DR   RefSeq; XP_012327408.1; XM_012471985.1.
DR   AlphaFoldDB; A0A2K5C6N6; -.
DR   STRING; 37293.ENSANAP00000004361; -.
DR   Ensembl; ENSANAT00000022115.1; ENSANAP00000004361.1; ENSANAG00000020271.1.
DR   GeneID; 105730646; -.
DR   CTD; 2330; -.
DR   GeneTree; ENSGT00940000160493; -.
DR   OMA; FMEWEHH; -.
DR   OrthoDB; 2079054at2759; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004031; F:aldehyde oxidase activity; IEA:Ensembl.
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   GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF78; FLAVIN-CONTAINING MONOOXYGENASE 5; 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|ARBA:ARBA00023136, 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        514..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   533 AA;  60345 MW;  52398FD0BF59F315 CRC64;
     MTKKRIAVIG GGVSGLSSIK CCLEEGLEPV CFERTDDIGG LWRFQENLEE GRASIYKSVI
     INTSKEMMCF SDYPIPDHYP NFMHNAQVLQ YFRMYAKEFD LLKYIRFKTT VCTVKKRPDF
     STSGQWEVVT ESEGKKETDV FDGVMVCTGH HTDAHLPLES FPGIEKFKGQ YFHSRDYKNP
     EGFTGKRVII IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGDYGY PFDVLFSSRL
     KYFMSKICGQ SLANTYLERQ MNQRFDHEMF GLKPKHRALS QHPTVNDELP NRIISGLVKV
     KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYTFAFPFLE DSVTVVKNKI SLYKKVFPPN
     LERPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKTLP SQSEMMAEIS KAQEEMEKRY
     VESQRHTIQG DYIDTMEELA DLVGVRPNLL ALAFTDPKLA LHLLLGPCTP IHYRLQGPGK
     WDEARKAILT TEDRIRKPLM TRAVEKSSSM TSTMTIGKFM LAVAFFAIII AYF
//
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