U78D2_ARATH
ID U78D2_ARATH Reviewed; 460 AA.
AC Q9LFJ8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Flavonol 3-O-glucosyltransferase;
DE EC=2.4.1.91 {ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:15807784, ECO:0000269|PubMed:23549747};
DE AltName: Full=Anthocyanin 3-O-glucosyltransferase {ECO:0000305};
DE AltName: Full=UDP glucose:flavonoid 3-O-glucosyltransferase {ECO:0000305};
DE AltName: Full=UDP-glycosyltransferase 78D2 {ECO:0000305};
GN Name=UGT78D2 {ECO:0000303|PubMed:11042215}; Synonyms=AGT {ECO:0000305};
GN OrderedLocusNames=At5g17050 {ECO:0000312|Araport:AT5G17050};
GN ORFNames=F2K13.200 {ECO:0000312|EMBL:CAC01718.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY.
RX PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 276:4338-4343(2001).
RN [5]
RP FUNCTION.
RX PubMed=11641410; DOI=10.1074/jbc.m109287200;
RA Lim E.K., Doucet C.J., Li Y., Elias L., Worrall D., Spencer S.P., Ross J.,
RA Bowles D.J.;
RT "The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-
RT hydroxybenzoic acid, and other benzoates.";
RL J. Biol. Chem. 277:586-592(2002).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15352060; DOI=10.1002/bit.20154;
RA Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.;
RT "Arabidopsis glycosyltransferases as biocatalysts in fermentation for
RT regioselective synthesis of diverse quercetin glucosides.";
RL Biotechnol. Bioeng. 87:623-631(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY PAP1.
RX PubMed=15807784; DOI=10.1111/j.1365-313x.2005.02371.x;
RA Tohge T., Nishiyama Y., Hirai M.Y., Yano M., Nakajima J., Awazuhara M.,
RA Inoue E., Takahashi H., Goodenowe D.B., Kitayama M., Noji M., Yamazaki M.,
RA Saito K.;
RT "Functional genomics by integrated analysis of metabolome and transcriptome
RT of Arabidopsis plants over-expressing an MYB transcription factor.";
RL Plant J. 42:218-235(2005).
RN [8]
RP FUNCTION.
RX PubMed=20085894; DOI=10.1093/mp/ssp071;
RA Pourcel L., Irani N.G., Lu Y., Riedl K., Schwartz S., Grotewold E.;
RT "The formation of anthocyanic vacuolar inclusions in Arabidopsis thaliana
RT and implications for the sequestration of anthocyanin pigments.";
RL Mol. Plant 3:78-90(2010).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23549747; DOI=10.1007/s00253-013-4844-7;
RA Kim H.J., Kim B.G., Ahn J.H.;
RT "Regioselective synthesis of flavonoid bisglycosides using Escherichia coli
RT harboring two glycosyltransferases.";
RL Appl. Microbiol. Biotechnol. 97:5275-5282(2013).
RN [10]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24251900; DOI=10.1111/nph.12558;
RA Yin R., Han K., Heller W., Albert A., Dobrev P.I., Zazimalova E.,
RA Schaeffner A.R.;
RT "Kaempferol 3-O-rhamnoside-7-O-rhamnoside is an endogenous flavonol
RT inhibitor of polar auxin transport in Arabidopsis shoots.";
RL New Phytol. 201:466-475(2014).
CC -!- FUNCTION: Flavonol 3-O-glucosyltransferase that catalyzes the transfer
CC of glucose from UDP-glucose to the 3-OH position of quercetin and
CC kaempferol (PubMed:15352060, PubMed:15807784, PubMed:23549747,
CC PubMed:24251900). Possesses high quercetin 3-O-glucosyltransferase
CC activity in vitro (PubMed:15352060, PubMed:23549747). Catalyzes the
CC glycosylation of anthocyanins from UDP-glucose (PubMed:20085894). Also
CC active in vitro on benzoates and benzoate derivatives
CC (PubMed:11641410). {ECO:0000269|PubMed:11641410,
CC ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:15807784,
CC ECO:0000269|PubMed:20085894, ECO:0000269|PubMed:23549747,
CC ECO:0000269|PubMed:24251900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-
CC glucoside + H(+) + UDP; Xref=Rhea:RHEA:22300, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16816, ChEBI:CHEBI:28802, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; EC=2.4.1.91;
CC Evidence={ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:15807784,
CC ECO:0000269|PubMed:23549747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22301;
CC Evidence={ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:15807784,
CC ECO:0000269|PubMed:23549747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=quercetin + UDP-alpha-D-glucose = H(+) + quercetin 3-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61180, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57694, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:144437; Evidence={ECO:0000269|PubMed:15352060,
CC ECO:0000269|PubMed:15807784, ECO:0000269|PubMed:23549747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61181;
CC Evidence={ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:15807784,
CC ECO:0000269|PubMed:23549747};
CC -!- PATHWAY: Flavonoid metabolism. {ECO:0000305}.
CC -!- INDUCTION: By PAP1. {ECO:0000269|PubMed:15807784}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype and altered flavonol glycoside
CC pattern (PubMed:24251900). The accumulation of kaempferol 3-O-
CC rhamnoside-7-O-rhamnoside in the mutant inhibits basipetal auxin
CC transport in the shoot, which correlates with the dwarf phenotype
CC (PubMed:24251900). {ECO:0000269|PubMed:24251900}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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; AL391141; CAC01718.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92377.1; -; Genomic_DNA.
DR EMBL; AY072325; AAL61932.1; -; mRNA.
DR EMBL; AY128739; AAM91139.1; -; mRNA.
DR PIR; T51560; T51560.
DR RefSeq; NP_197207.1; NM_121711.5.
DR AlphaFoldDB; Q9LFJ8; -.
DR SMR; Q9LFJ8; -.
DR STRING; 3702.AT5G17050.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q9LFJ8; -.
DR PaxDb; Q9LFJ8; -.
DR PRIDE; Q9LFJ8; -.
DR ProteomicsDB; 243209; -.
DR EnsemblPlants; AT5G17050.1; AT5G17050.1; AT5G17050.
DR GeneID; 831568; -.
DR Gramene; AT5G17050.1; AT5G17050.1; AT5G17050.
DR KEGG; ath:AT5G17050; -.
DR Araport; AT5G17050; -.
DR TAIR; locus:2148126; AT5G17050.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_2_1; -.
DR InParanoid; Q9LFJ8; -.
DR OMA; IKPFNVR; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9LFJ8; -.
DR BioCyc; ARA:AT5G17050-MON; -.
DR BioCyc; MetaCyc:AT5G17050-MON; -.
DR PRO; PR:Q9LFJ8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFJ8; baseline and differential.
DR Genevisible; Q9LFJ8; AT.
DR GO; GO:0047213; F:anthocyanidin 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0102360; F:daphnetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047893; F:flavonol 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102425; F:myricetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phenylpropanoid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..460
FT /note="Flavonol 3-O-glucosyltransferase"
FT /id="PRO_0000285275"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 286
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 338..341
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 356..364
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT BINDING 380..381
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9LNE6"
SQ SEQUENCE 460 AA; 50486 MW; E9DEAD19E4E05188 CRC64;
MTKPSDPTRD SHVAVLAFPF GTHAAPLLTV TRRLASASPS TVFSFFNTAQ SNSSLFSSGD
EADRPANIRV YDIADGVPEG YVFSGRPQEA IELFLQAAPE NFRREIAKAE TEVGTEVKCL
MTDAFFWFAA DMATEINASW IAFWTAGANS LSAHLYTDLI RETIGVKEVG ERMEETIGVI
SGMEKIRVKD TPEGVVFGNL DSVFSKMLHQ MGLALPRATA VFINSFEDLD PTLTNNLRSR
FKRYLNIGPL GLLSSTLQQL VQDPHGCLAW MEKRSSGSVA YISFGTVMTP PPGELAAIAE
GLESSKVPFV WSLKEKSLVQ LPKGFLDRTR EQGIVVPWAP QVELLKHEAT GVFVTHCGWN
SVLESVSGGV PMICRPFFGD QRLNGRAVEV VWEIGMTIIN GVFTKDGFEK CLDKVLVQDD
GKKMKCNAKK LKELAYEAVS SKGRSSENFR GLLDAVVNII
