ID   A0A067KNI0_JATCU        Unreviewed;       421 AA.
AC   A0A067KNI0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   ORFNames=JCGZ_12913 {ECO:0000313|EMBL:KDP33364.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP33364.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP33364.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP33364.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
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|RuleBase:RU361177}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK914543; KDP33364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067KNI0; -.
DR   STRING; 180498.A0A067KNI0; -.
DR   Proteomes; UP000027138; 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   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR   PANTHER; PTHR43539:SF49; INDOLE-3-PYRUVATE MONOOXYGENASE YUCCA3-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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:UP000027138}.
SQ   SEQUENCE   421 AA;  47155 MW;  5A53F7624C87DD4E CRC64;
     MFQSSPQEDF LSRRCVWVNG PVIVGAGPSG LAVGAGLKQQ GVPFIILERA NCIASLWQTR
     TYDRLKLHLP KQFCQLPNFP FPEDFPEYPT KYQFISYLES YAKHYDITPQ FNETVQSAKY
     DETFGLWRVK TISIITGSIS TEVEYICRWL VVATGENAEK VVPEFEGVQE FGGNIMHACD
     YKSGQNYSGK RVLVVGCGNS GMEISLDLCN HKASPSMVVR SSVHVLPREI FGNSTFELAV
     TLMNWLPLWL VDKILLILAW LILGNLEKFG LKRPFIGPLQ LKNSEGKTPV LDIGALDKIR
     SGQIKVVPGI KRFFNGRVEL VNGEKLEIDS VILATGYRSN VPSWLRENEF FSEDGIPKNP
     FPNGWKGKAG LYAVGFTRRG LSGASLDAIS VALDIAKSWK EETKQKKKTV AARHRRCISH
     F
//