ID YUC8_ARATH Reviewed; 426 AA.
AC Q9SVU0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 150.
DE RecName: Full=Probable indole-3-pyruvate monooxygenase YUCCA8;
DE EC=1.14.13.168;
DE AltName: Full=Flavin-containing monooxygenase YUCCA8;
GN Name=YUC8; Synonyms=BAS3, YUCCA8; OrderedLocusNames=At4g28720;
GN ORFNames=F16A16.170;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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 BY RVE1, AND TISSUE SPECIFICITY.
RX PubMed=19805390; DOI=10.1073/pnas.0813035106;
RA Rawat R., Schwartz J., Jones M.A., Sairanen I., Cheng Y., Andersson C.R.,
RA Zhao Y., Ljung K., Harmer S.L.;
RT "REVEILLE1, a Myb-like transcription factor, integrates the circadian clock
RT and auxin pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16883-16888(2009).
RN [7]
RP INDUCTION BY STY1.
RX PubMed=20154152; DOI=10.1105/tpc.108.064816;
RA Eklund D.M., Staaldal V., Valsecchi I., Cierlik I., Eriksson C.,
RA Hiratsu K., Ohme-Takagi M., Sundstroem J.F., Thelander M., Ezcurra I.,
RA Sundberg E.;
RT "The Arabidopsis thaliana STYLISH1 protein acts as a transcriptional
RT activator regulating auxin biosynthesis.";
RL Plant Cell 22:349-363(2010).
RN [8]
RP FUNCTION.
RX PubMed=22025721; DOI=10.1073/pnas.1108436108;
RA Won C., Shen X., Mashiguchi K., Zheng Z., Dai X., Cheng Y., Kasahara H.,
RA Kamiya Y., Chory J., Zhao Y.;
RT "Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN
RT AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18518-18523(2011).
RN [9]
RP INDUCTION BY HIGH TEMPERATURE.
RX PubMed=22479194; DOI=10.1371/journal.pgen.1002594;
RA Sun J., Qi L., Li Y., Chu J., Li C.;
RT "PIF4-mediated activation of YUCCA8 expression integrates temperature into
RT the auxin pathway in regulating arabidopsis hypocotyl growth.";
RL PLoS Genet. 8:E1002594-E1002594(2012).
CC -!- FUNCTION: Involved in auxin biosynthesis. Belongs to the set of
CC redundant YUCCA genes probably responsible for auxin biosynthesis in
CC roots. {ECO:0000269|PubMed:22025721}.
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 -!- TISSUE SPECIFICITY: Expressed in root tips and in hydathodes. Expressed
CC in root vasculature and quiescent center, but not in the meristematic
CC zone of the root tip. {ECO:0000269|PubMed:19805390}.
CC -!- INDUCTION: Up-regulated by high temperature via activation by PIF4.
CC Positively regulated by STY1 and during the day by REV1.
CC {ECO:0000269|PubMed:19805390, ECO:0000269|PubMed:20154152,
CC ECO:0000269|PubMed:22479194}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AL035353; CAA22980.1; -; Genomic_DNA.
DR EMBL; AL161573; CAB81460.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85534.1; -; Genomic_DNA.
DR EMBL; BT029238; ABJ98570.1; -; mRNA.
DR PIR; T04527; T04527.
DR RefSeq; NP_194601.1; NM_119016.3.
DR AlphaFoldDB; Q9SVU0; -.
DR SMR; Q9SVU0; -.
DR BioGRID; 14280; 5.
DR IntAct; Q9SVU0; 5.
DR STRING; 3702.Q9SVU0; -.
DR PaxDb; 3702-AT4G28720-1; -.
DR ProteomicsDB; 232328; -.
DR EnsemblPlants; AT4G28720.1; AT4G28720.1; AT4G28720.
DR GeneID; 828993; -.
DR Gramene; AT4G28720.1; AT4G28720.1; AT4G28720.
DR KEGG; ath:AT4G28720; -.
DR Araport; AT4G28720; -.
DR TAIR; AT4G28720; YUC8.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_2_0_1; -.
DR InParanoid; Q9SVU0; -.
DR OMA; NTMGKTP; -.
DR OrthoDB; 5488474at2759; -.
DR PhylomeDB; Q9SVU0; -.
DR UniPathway; UPA00151; -.
DR PRO; PR:Q9SVU0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVU0; baseline and differential.
DR Genevisible; Q9SVU0; AT.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IDA:TAIR.
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; TAS:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0010600; P:regulation of auxin biosynthetic process; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
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 PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR PANTHER; PTHR43539:SF11; INDOLE-3-PYRUVATE MONOOXYGENASE YUCCA8-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 2: Evidence at transcript level;
KW Auxin biosynthesis; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..426
FT /note="Probable indole-3-pyruvate monooxygenase YUCCA8"
FT /id="PRO_0000400075"
FT BINDING 29..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 199..204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 426 AA; 48110 MW; 875A73059446321C CRC64;
MENMFRLMDQ DQDLTNNRCI WVNGPVIVGA GPSGLATAAC LHEQNVPFVV LERADCIASL
WQKRTYDRLK LHLPKQFCQL PKMPFPEDFP EYPTKRQFID YLESYATRFE INPKFNECVQ
TARFDETSGL WRVKTVSKSE STQTEVEYIC RWLVVATGEN AERVMPEIDG LSEFSGEVIH
ACDYKSGEKF AGKKVLVVGC GNSGMEVSLD LANHFAKPSM VVRSSLHVMP REVMGKSTFE
LAMKMLRWFP LWLVDKILLV LSWMVLGNIE KYGLKRPEMG PMELKSVKGK TPVLDIGAIE
KIRLGKINVV PGIKRFNGNK VELVNGEQLD VDSVVLATGY RSNVPYWLQE NEFFAKNGFP
KTVADNNGWK GRTGLYAVGF TRKGLSGASM DAVKIAQDIG SVWQLETKQP TKRSRGSLRR
CISQQF
//
