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Database: UniProt
Entry: D7MV98_ARALL
LinkDB: D7MV98_ARALL
Original site: D7MV98_ARALL 
ID   D7MV98_ARALL            Unreviewed;       415 AA.
AC   D7MV98;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   ORFNames=ARALYDRAFT_332994 {ECO:0000313|EMBL:EFH39408.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate +
CC         CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.13.168;
CC         Evidence={ECO:0000256|ARBA:ARBA00035920};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361177};
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004814}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC       ECO:0000256|RuleBase:RU361177}.
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DR   EMBL; GL348721; EFH39408.1; -; Genomic_DNA.
DR   RefSeq; XP_002863149.1; XM_002863103.1.
DR   AlphaFoldDB; D7MV98; -.
DR   STRING; 81972.D7MV98; -.
DR   EnsemblPlants; fgenesh1_pm.C_scaffold_9000022; fgenesh1_pm.C_scaffold_9000022; fgenesh1_pm.C_scaffold_9000022.
DR   GeneID; 9299225; -.
DR   Gramene; fgenesh1_pm.C_scaffold_9000022; fgenesh1_pm.C_scaffold_9000022; fgenesh1_pm.C_scaffold_9000022.
DR   KEGG; aly:9299225; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_2_0_1; -.
DR   OrthoDB; 5488474at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:RHEA.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009723; P:response to ethylene; IEA:EnsemblPlants.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR   PANTHER; PTHR43539:SF36; INDOLE-3-PYRUVATE MONOOXYGENASE YUCCA2; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Auxin biosynthesis {ECO:0000256|ARBA:ARBA00023070};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361177};
KW   Monooxygenase {ECO:0000256|RuleBase:RU361177};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361177};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
SQ   SEQUENCE   415 AA;  46730 MW;  03CE40EA273EF6FE CRC64;
     MEFVTETLGK RVHDPYVEET RFLMIPGPII VGSGPSGLAT AACLKSRDIP SLILERSTCI
     ASLWQLKTYD RLRLHLPKHF CELPLMPFPS SYPTYPTKQQ FVQYLESYAE HFDLKPVFNQ
     TVEEAKFDRQ RGLWRVRTTV GKKDETMEYL SRWLVVATGE NAEEVMPEID GIADFGGPIL
     HTSSYKSGEM FSEKKVLVVG CGNSGMEVCL DLYNFNAHPS LVVRDSVHVL PQEMLGISTF
     GISTSLLKWF PVQVVDRFLL RMSRLVLGDT DRLGLVRPKL GPLERKIKCG KTPVLDVGTL
     AKIRSGHIKV YPELKRVMHH SAEFVDGRVD NFDAIILATG YKSNVPMWLK GMNMFCEKDG
     FPYKPFPNGW KGESGLYAVG FTKLGLLGAA IDAKKIAEDI EVQRNFLPLA RPQHC
//
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