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Database: UniProt
Entry: C3ZTI6_BRAFL
LinkDB: C3ZTI6_BRAFL
Original site: C3ZTI6_BRAFL 
ID   C3ZTI6_BRAFL            Unreviewed;       531 AA.
AC   C3ZTI6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   ORFNames=BRAFLDRAFT_113828 {ECO:0000313|EMBL:EEN44233.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN44233.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN44233.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN44233.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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|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|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   EMBL; GG666677; EEN44233.1; -; Genomic_DNA.
DR   RefSeq; XP_002588222.1; XM_002588176.1.
DR   AlphaFoldDB; C3ZTI6; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   InParanoid; C3ZTI6; -.
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; IBA:GO_Central.
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; 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: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   3: Inferred from homology;
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|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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        509..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   531 AA;  60449 MW;  6045D41387C66629 CRC64;
     MSKKVAVIGS GASGLAAIKC CLDEGLQPVC FEKGTDIGGL WNFKEEALPG FASVYRSTVI
     NTSKEMMCYS DFPIPKEYPN FMHHSWVIKY FRLYADNFGL MKYIRFGHHI DHVKPREDFQ
     ETGQWDVTYT DEEKNETTTE MYDAVMVCTG HHVYPHYPRD SFPGIDDFQG KTMHSHDYKD
     QHGFENKRVV IIGIGNSGGD IAVELSRHAK QVYLSTRRGT WVINRISEGG LPIDIIGNRR
     LLNGVPSSLK EAAGRRQLNQ RFDHALYGLQ PEHNVFGQHP MVNDDMPNRI ITGSLVIKPN
     IKRFTKTGVI FDNDTVEDDI DIVVFATGYR FDFPFVDKSV MKVENNQVNL YKYVFPPKLD
     PPTLSIIGLI QPLGAIMPIS EMQCRWATRV FKGTTKLPPQ GAMFDNIRQK KMEMSKRYYN
     TPRHTIQVDY IGIMDEIAEQ IGVKPDLKRL LLSDPRLALT VFAGPCTPYQ YRLMGPGAWK
     GAKEAIETQW DRITYPTKTR PVPKQTTNGV PGILKLLIVM VLIVAFIWRL L
//
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