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Database: UniProt
Entry: M8BTC4_AEGTA
LinkDB: M8BTC4_AEGTA
Original site: M8BTC4_AEGTA 
ID   M8BTC4_AEGTA            Unreviewed;       382 AA.
AC   M8BTC4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=indole-3-pyruvate monooxygenase {ECO:0000256|ARBA:ARBA00039148};
DE            EC=1.14.13.168 {ECO:0000256|ARBA:ARBA00039148};
OS   Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=37682 {ECO:0000313|EnsemblPlants:EMT10089};
RN   [1] {ECO:0000313|EnsemblPlants:EMT10089}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   AlphaFoldDB; M8BTC4; -.
DR   SMR; M8BTC4; -.
DR   EnsemblPlants; EMT10089; EMT10089; F775_11723.
DR   OMA; KELIWYG; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR43539:SF92; -; 1.
DR   PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   382 AA;  41617 MW;  18F4198C27AC9D53 CRC64;
     MENVVVLIVG AGPAGLATAA CLSQFSIPYV IVERESCSAS LWRNHAYNRL KLHLAKEFCE
     LPHMSYPVDA PTYIPKTLFV KYLDDYVERF NIQPKYLTSV ESSTYDNDQQ CWSIVAHDMA
     KSTIVRFSAK FLVVASGENS AENIPMIPGL QSFPGDVVHS SSYKSGKSYS GMNVLVIGSG
     NSGMEIAYDL AAHGANTSIV IRSPIHIMTK ELIRLGMTLA RHLPLNLVDN LIVMAANLKF
     GDLSKHGIRR PKMGPMILKS KTGRSAVIDV GTVGLIKKGI IKVHGSISKI MGDIVEFQCS
     KEISFDAIVF ATGYKSTTNI WLTNGERMLN ENGLPIKEYP NHWKGENGLY CVGLARRGLA
     GIAADAKNIA GDIKSVICTM SG
//
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