ID A0A368S9U8_SETIT Unreviewed; 379 AA.
AC A0A368S9U8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=indole-3-pyruvate monooxygenase {ECO:0000256|ARBA:ARBA00039148};
DE EC=1.14.13.168 {ECO:0000256|ARBA:ARBA00039148};
GN ORFNames=SETIT_8G204700v2 {ECO:0000313|EMBL:RCV39207.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV39207.1};
RN [1] {ECO:0000313|EMBL:RCV39207.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV39207.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV39207.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV39207.1};
RA Noorani M.;
RL Submitted (JUL-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};
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; CM003535; RCV39207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368S9U8; -.
DR STRING; 4555.A0A368S9U8; -.
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; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR PANTHER; PTHR43539:SF30; OS11G0207700 PROTEIN; 1.
DR Pfam; PF13738; Pyr_redox_3; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 379 AA; 41632 MW; 127755E920E14C22 CRC64;
MVLIVGAGPA GLATAACLTQ LSIPYVIVER EYCSASLWRN RAYDRLKLHL AKEFCELPHM
SYPADAPTYI PKDQFVKYLD SYIECFNIRP KYHTAIESCT YDEARRCWLG VAHDMKTSVS
VRYMARFLVV ASGENSAENI PVIPGLHCFT GETIHSSRYK SGATYSGKNV LVVGCGNSGM
EIAYDLASHG ANTSIVIRSP VHVTTKEIIR LGMTLVQHTP VNVVDDLLVR LSNYVFGDLS
RHGIVRPKMG PLLLKEKIGR SAVIDVGTVG LIKKGTIKVL GNISKIKGKI VEFEDRNEDT
FDAIVFATGY KSTANTWLKN GESMLNNDGL PKKEFPNHWK GENGLYCAGL AKRGLAGIAM
DAKNIANDIL SCLASMHDI
//