ID   A0A1D6PS54_MAIZE        Unreviewed;       789 AA.
AC   A0A1D6PS54;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=indole-3-pyruvate monooxygenase {ECO:0000256|ARBA:ARBA00039148};
DE            EC=1.14.13.168 {ECO:0000256|ARBA:ARBA00039148};
GN   ORFNames=ZEAMMB73_Zm00001d049077 {ECO:0000313|EMBL:AQK49539.1};
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:AQK49539.1};
RN   [1] {ECO:0000313|EMBL:AQK49539.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK49539.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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; CM000780; AQK49539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6PS54; -.
DR   SMR; A0A1D6PS54; -.
DR   STRING; 4577.A0A1D6PS54; -.
DR   PaxDb; 4577-GRMZM2G333035_P01; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   InParanoid; A0A1D6PS54; -.
DR   OMA; NGENHYV; -.
DR   ExpressionAtlas; A0A1D6PS54; baseline.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR   PANTHER; PTHR43539:SF50; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF13738; Pyr_redox_3; 2.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 4.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000313|EMBL:AQK49539.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:AQK49539.1}.
SQ   SEQUENCE   789 AA;  87097 MW;  0143628077D89DF1 CRC64;
     MELVVLIVGA GPAGLATAAC LSQRSIPYLI VEREDCSASL WRYRTYDRVK LHLSKEFSCL
     PYMPHEEDTP TYIPKAEFLK YLDCYREHFG IKPRYCTSVV SAAYDEGTGR WVVAARDTVE
     GTEIRYAARF LVVATGENGA GRIPEIQGLE SFCGEAIHSS TYKSGRSYAG RRVLVVGAGN
     SGMEIAYDLA NHGADTSIVV RSPVHIMPKE LIRLGMTFVQ YMPVTIVDLF LVKLADFIFG
     DLSNYGIVRP GVGPLQLKSK TGRSSVIDVG TAGLIKKGVV KVFKRISKIT GNKVQFECGK
     DCEFDAIVFA TGYKSSANLW LKHILKKDKE KESFGGSTKF LHSYSILASN FVPKDKVTVE
     LAVSCESSTR DPVYKPHKTL WSSSTVNGCR LDISRSSERR LLHCTHPART EKMELVVLIV
     GAGPAGLATA ACLSQRSIPY LIVEREDCSA SLWRYRTYDR VKLHLSKEFS CLPYMPHEED
     TPTYIPKAEF LKYLDCYREH FGIKPRYCTC VVSAAYDEGT GRWVVAARDT VEGTEIRYAA
     RFLVVATGEN GAGRIPEIQG LESFCGEAIH SSTYKSGKSY AGRRVLVVGA GNSGMEIAYD
     LANHGADTSI VVRSPVHIMP KELIRLGMTF VQYMPVTIVD LFLVKLADFI FGDLSNYGIV
     RPGVGPLQLK SKTGRSSVID VGTAGLIKKG VVKVFKRISK ITGNKVQFEC GKDCEFDAIV
     FATGYKSSAN LWLKADDKCM VNSDGRPNTC RPNIWKGENG LYFSGFRRMG LAGICMDAYN
     IANEIVSVY
//