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 27-MAR-2024, entry version 133. 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}; GN 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.Q9LFJ8; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR iPTMnet; Q9LFJ8; -. DR PaxDb; 3702-AT5G17050-1; -. 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; AT5G17050; UGT78D2. DR eggNOG; KOG1192; Eukaryota. DR HOGENOM; CLU_001724_0_2_1; -. DR InParanoid; Q9LFJ8; -. DR OMA; CTLSLYF; -. DR OrthoDB; 382054at2759; -. DR PhylomeDB; Q9LFJ8; -. DR BioCyc; ARA:AT5G17050-MONOMER; -. DR BioCyc; MetaCyc:AT5G17050-MONOMER; -. DR PRO; PR:Q9LFJ8; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9LFJ8; baseline and differential. 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR002213; UDP_glucos_trans. DR InterPro; IPR035595; UDP_glycos_trans_CS. DR PANTHER; PTHR48049:SF29; FLAVONOL 3-O-GLUCOSYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR48049; GLYCOSYLTRANSFERASE; 1. DR Pfam; PF00201; UDPGT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00375; UDPGT; 1. DR Genevisible; Q9LFJ8; AT. 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 ACT_SITE 23 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT ACT_SITE 123 FT /note="Charge relay" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 23 FT /ligand="an anthocyanidin" FT /ligand_id="ChEBI:CHEBI:143576" FT /evidence="ECO:0000250|UniProtKB:P51094" FT BINDING 88 FT /ligand="an anthocyanidin" FT /ligand_id="ChEBI:CHEBI:143576" FT /evidence="ECO:0000250|UniProtKB:P51094" FT BINDING 145 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 154 FT /ligand="an anthocyanidin" FT /ligand_id="ChEBI:CHEBI:143576" FT /evidence="ECO:0000250|UniProtKB:P51094" FT BINDING 339 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 341 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 356 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 359 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 360 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 361 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 364 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 379 FT /ligand="an anthocyanidin" FT /ligand_id="ChEBI:CHEBI:143576" FT /evidence="ECO:0000250|UniProtKB:P51094" FT BINDING 380 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 381 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" 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 //