YUC11_ARATH
ID YUC11_ARATH Reviewed; 391 AA.
AC Q9LPL3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable indole-3-pyruvate monooxygenase YUCCA11;
DE EC=1.14.13.168;
DE AltName: Full=Flavin-containing monooxygenase YUCCA11;
GN Name=YUC11; Synonyms=YUCCA11; OrderedLocusNames=At1g21430;
GN ORFNames=F24J8.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16818609; DOI=10.1101/gad.1415106;
RA Cheng Y., Dai X., Zhao Y.;
RT "Auxin biosynthesis by the YUCCA flavin monooxygenases controls the
RT formation of floral organs and vascular tissues in Arabidopsis.";
RL Genes Dev. 20:1790-1799(2006).
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17704214; DOI=10.1105/tpc.107.053009;
RA Cheng Y., Dai X., Zhao Y.;
RT "Auxin synthesized by the YUCCA flavin monooxygenases is essential for
RT embryogenesis and leaf formation in Arabidopsis.";
RL Plant Cell 19:2430-2439(2007).
RN [5]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17461789; DOI=10.1111/j.1365-313x.2007.03101.x;
RA Hansen B.G., Kliebenstein D.J., Halkier B.A.;
RT "Identification of a flavin-monooxygenase as the S-oxygenating enzyme in
RT aliphatic glucosinolate biosynthesis in Arabidopsis.";
RL Plant J. 50:902-910(2007).
RN [6]
RP INDUCTION.
RX PubMed=22109847; DOI=10.1007/s00425-011-1552-3;
RA Lee M., Jung J.H., Han D.Y., Seo P.J., Park W.J., Park C.M.;
RT "Activation of a flavin monooxygenase gene YUCCA7 enhances drought
RT resistance in Arabidopsis.";
RL Planta 235:923-938(2012).
CC -!- FUNCTION: Involved in auxin biosynthesis.
CC {ECO:0000269|PubMed:17704214}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- DEVELOPMENTAL STAGE: Expression relatively broad during early stages of
CC embryogenesis and more restricted to discrete groups of cells in mature
CC embryos. Later, expression mainly restricted to the cotyledons and the
CC apical meristem. {ECO:0000269|PubMed:17704214}.
CC -!- INDUCTION: Up-regulated by drought. {ECO:0000269|PubMed:22109847}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AC015447; AAF87896.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30101.1; -; Genomic_DNA.
DR PIR; C86347; C86347.
DR RefSeq; NP_173564.1; NM_101994.1.
DR AlphaFoldDB; Q9LPL3; -.
DR SMR; Q9LPL3; -.
DR STRING; 3702.AT1G21430.1; -.
DR PaxDb; Q9LPL3; -.
DR PRIDE; Q9LPL3; -.
DR EnsemblPlants; AT1G21430.1; AT1G21430.1; AT1G21430.
DR GeneID; 838741; -.
DR Gramene; AT1G21430.1; AT1G21430.1; AT1G21430.
DR KEGG; ath:AT1G21430; -.
DR Araport; AT1G21430; -.
DR TAIR; locus:2026967; AT1G21430.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_2_1_1; -.
DR InParanoid; Q9LPL3; -.
DR OMA; VEHFNIC; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q9LPL3; -.
DR UniPathway; UPA00151; -.
DR PRO; PR:Q9LPL3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPL3; baseline and differential.
DR Genevisible; Q9LPL3; AT.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
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-UniPathway.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 2: Evidence at transcript level;
KW Auxin biosynthesis; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..391
FT /note="Probable indole-3-pyruvate monooxygenase YUCCA11"
FT /id="PRO_0000400078"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 180..185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 391 AA; 43358 MW; FA67FB53561B96ED CRC64;
MEKEIKILVL IIGAGPAGLA TSACLNRLNI PNIVVERDVC SASLWKRRSY DRLKLHLAKQ
FCQLPHMPFP SNTPTFVSKL GFINYLDEYA TRFNVNPRYN RNVKSAYFKD GQWIVKVVNK
TTALIEVYSA KFMVAATGEN GEGVIPEIPG LVESFQGKYL HSSEYKNGEK FAGKDVLVVG
CGNSGMEIAY DLSKCNANVS IVVRSQVHVL TRCIVRIGMS LLRFFPVKLV DRLCLLLAEL
RFRNTSRYGL VRPNNGPFLN KLITGRSATI DVGCVGEIKS GKIQVVTSIK RIEGKTVEFI
DGNTKNVDSI VFATGYKSSV SKWLEVDDGD LFNENGMPKR EFPDHWKGKN GLYSAGFGKQ
GLAGISRDAR NIARDIDSLV CGRSSKNKLS K
