ID   A1YHR5_MAIZE            Unreviewed;       398 AA.
AC   A1YHR5;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=indole-3-pyruvate monooxygenase {ECO:0000256|ARBA:ARBA00039148};
DE            EC=1.14.13.168 {ECO:0000256|ARBA:ARBA00039148};
GN   Name=yuc {ECO:0000313|EMBL:ABL61263.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ABL61263.1};
RN   [1] {ECO:0000313|EMBL:ABL61263.1}
RP   NUCLEOTIDE SEQUENCE.
RA   LeClere S.L., Schmelz E.A., Chourey P.S.;
RT   "The maize miniature seed mutant displays altered sugar accumulation and
RT   decreased tryptophan-dependant auxin biosynthesis in developing kernels.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AET34453.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Li Q.-B., Chourey P.;
RT   "Isolation, characterization, and expression analyses of flavin
RT   monooxygenase (yuc) gene in maize.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; DQ995287; ABL61263.1; -; mRNA.
DR   EMBL; JN815079; AET34453.1; -; mRNA.
DR   RefSeq; NP_001105991.1; NM_001112521.1.
DR   AlphaFoldDB; A1YHR5; -.
DR   SMR; A1YHR5; -.
DR   GeneID; 100037821; -.
DR   KEGG; zma:100037821; -.
DR   OrthoDB; 348824at2759; -.
DR   ExpressionAtlas; A1YHR5; baseline and differential.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR   PANTHER; PTHR43539:SF9; INDOLE-3-PYRUVATE MONOOXYGENASE YUCCA11-RELATED; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
KW   Monooxygenase {ECO:0000313|EMBL:ABL61263.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   398 AA;  43547 MW;  9C69444A107598F1 CRC64;
     MTEKVLVLIV GAGPSGLAVA ACLGEHGIPY HIVEREDCSA SLWRKRTYDR LKLHLAKEFC
     ELPRMSHPSD APKYITREQF VRYVDDYVER FNILPRYSTS VESCEYDEAS GRWDVRARDL
     ADGGGRVAEY TARFLVVATG ENCEGVIPDI PGLRDFPAGE VVHSSSYKSW KNYAGKRVLV
     VGCGNSGMEI AYDLAYNGVE TSLVIRSPVH VMTKGLIYLG MRLLKWHLPV KLVDFIILTL
     ANIQFGDLSR YGIVRPDMGP LLLKAKTGRS AVLDVGTTQL IKTGDIKVVG AISRIRGNTV
     EFEDGKERDF DSLVFATGYR STANTWLKDG GSLLDDNGMP KKKAGLQQGS RPWKGGNGLY
     CVGLGMAGLA GISRDAVSVA ADIKAAVDSM VGPPAFWF
//