U84A3_ARATH
ID U84A3_ARATH Reviewed; 479 AA.
AC O23401; Q8LB44;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=UDP-glycosyltransferase 84A3 {ECO:0000303|PubMed:11042215};
DE EC=2.4.1.120 {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:11187886};
DE EC=2.4.1.177 {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:11187886};
DE AltName: Full=Hydroxycinnamate glucosyltransferase 3 {ECO:0000303|PubMed:11187886};
DE Short=AtHCAGT3 {ECO:0000303|PubMed:11187886};
GN Name=UGT84A3 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At4g15490 {ECO:0000312|Araport:AT4G15490};
GN ORFNames=dl3785c {ECO:0000312|EMBL:CAB10327.1},
GN FCAALL.17 {ECO:0000312|EMBL:CAB78591.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11187886; DOI=10.1016/s0014-5793(00)02270-5;
RA Milkowski C., Baumert A., Strack D.;
RT "Identification of four Arabidopsis genes encoding hydroxycinnamate
RT glucosyltransferases.";
RL FEBS Lett. 486:183-184(2000).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11042211; DOI=10.1074/jbc.m007263200;
RA Lim E.K., Li Y., Parr A., Jackson R., Ashford D.A., Bowles D.J.;
RT "Identification of glucosyltransferase genes involved in sinapate
RT metabolism and lignin synthesis in Arabidopsis.";
RL J. Biol. Chem. 276:4344-4349(2001).
CC -!- FUNCTION: UDP-glucosyltransferase that forms glucose esters with
CC phenylpropanoids (PubMed:11042211, PubMed:11187886). Glucosylates 4-
CC coumarate, ferulate, caffeate, sinapate and cinnamate (PubMed:11042211,
CC PubMed:11187886). {ECO:0000269|PubMed:11042211,
CC ECO:0000269|PubMed:11187886}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-
CC trans-4-coumarate + H(+) + UDP; Xref=Rhea:RHEA:21636,
CC ChEBI:CHEBI:12876, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:79066;
CC Evidence={ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:11187886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-ferulate + UDP-alpha-D-glucose = 1-O-[(E)-feruloyl]-beta-
CC D-glucose + UDP; Xref=Rhea:RHEA:57468, ChEBI:CHEBI:29749,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:81321;
CC Evidence={ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:11187886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeate + UDP-alpha-D-glucose = 1-O-[(E)-caffeoyl]-beta-
CC D-glucose + UDP; Xref=Rhea:RHEA:57464, ChEBI:CHEBI:614,
CC ChEBI:CHEBI:57770, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC Evidence={ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:11187886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=E-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-
CC D-glucose + UDP; Xref=Rhea:RHEA:13305, ChEBI:CHEBI:16546,
CC ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.120; Evidence={ECO:0000269|PubMed:11042211,
CC ECO:0000269|PubMed:11187886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-
CC beta-D-glucose + UDP; Xref=Rhea:RHEA:13437, ChEBI:CHEBI:15669,
CC ChEBI:CHEBI:16279, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.177; Evidence={ECO:0000269|PubMed:11042211,
CC ECO:0000269|PubMed:11187886};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for 4-coumarate {ECO:0000269|PubMed:11042211};
CC KM=240 uM for ferulate {ECO:0000269|PubMed:11042211};
CC KM=580 uM for sinapate {ECO:0000269|PubMed:11042211};
CC KM=810 uM for cinnamate {ECO:0000269|PubMed:11042211};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z97339; CAB10327.1; -; Genomic_DNA.
DR EMBL; AL161541; CAB78591.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83610.1; -; Genomic_DNA.
DR EMBL; AY057646; AAL15277.1; -; mRNA.
DR EMBL; AY074339; AAL67035.1; -; mRNA.
DR EMBL; AY142676; AAN13214.1; -; mRNA.
DR EMBL; AY087431; AAM64979.1; -; mRNA.
DR PIR; E71419; E71419.
DR RefSeq; NP_193284.1; NM_117639.3.
DR AlphaFoldDB; O23401; -.
DR SMR; O23401; -.
DR STRING; 3702.AT4G15490.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; O23401; -.
DR PRIDE; O23401; -.
DR ProteomicsDB; 242614; -.
DR EnsemblPlants; AT4G15490.1; AT4G15490.1; AT4G15490.
DR GeneID; 827221; -.
DR Gramene; AT4G15490.1; AT4G15490.1; AT4G15490.
DR KEGG; ath:AT4G15490; -.
DR Araport; AT4G15490; -.
DR TAIR; locus:2130215; AT4G15490.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; O23401; -.
DR OMA; GYPWWSD; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; O23401; -.
DR BioCyc; ARA:AT4G15490-MON; -.
DR SABIO-RK; O23401; -.
DR PRO; PR:O23401; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23401; baseline and differential.
DR Genevisible; O23401; AT.
DR GO; GO:0050412; F:cinnamate beta-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047218; F:hydroxycinnamate 4-beta-glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0050284; F:sinapate 1-glucosyltransferase activity; ISS:TAIR.
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; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="UDP-glycosyltransferase 84A3"
FT /id="PRO_0000409122"
FT BINDING 289
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 344..346
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 361..369
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 383..386
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT CONFLICT 44
FT /note="K -> Q (in Ref. 5; AAM64979)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="F -> L (in Ref. 5; AAM64979)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="M -> I (in Ref. 5; AAM64979)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="S -> G (in Ref. 5; AAM64979)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="F -> L (in Ref. 5; AAM64979)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="G -> S (in Ref. 5; AAM64979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 53913 MW; 369CC944AE5E0DE6 CRC64;
MDPSRHTHVM LVSFPGQGHV NPLLRLGKLI ASKGLLVTFV TTEKPWGKKM RQANKIQDGV
LKPVGLGFIR FEFFSDGFAD DDEKRFDFDA FRPHLEAVGK QEIKNLVKRY NKEPVTCLIN
NAFVPWVCDV AEELHIPSAV LWVQSCACLT AYYYYHHRLV KFPTKTEPDI SVEIPCLPLL
KHDEIPSFLH PSSPYTAFGD IILDQLKRFE NHKSFYLFID TFRELEKDIM DHMSQLCPQA
IISPVGPLFK MAQTLSSDVK GDISEPASDC MEWLDSREPS SVVYISFGTI ANLKQEQMEE
IAHGVLSSGL SVLWVVRPPM EGTFVEPHVL PRELEEKGKI VEWCPQERVL AHPAIACFLS
HCGWNSTMEA LTAGVPVVCF PQWGDQVTDA VYLADVFKTG VRLGRGAAEE MIVSREVVAE
KLLEATVGEK AVELRENARR WKAEAEAAVA DGGSSDMNFK EFVDKLVTKH VTREDNGEH
