U84A1_ARATH
ID U84A1_ARATH Reviewed; 490 AA.
AC Q5XF20; O23400; Q8H0V7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=UDP-glycosyltransferase 84A1 {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 2 {ECO:0000303|PubMed:11187886};
DE Short=AtHCAGT2 {ECO:0000303|PubMed:11187886};
GN Name=UGT84A1 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At4g15480 {ECO:0000312|Araport:AT4G15480};
GN ORFNames=dl3780c {ECO:0000312|EMBL:CAB10326.1},
GN FCAALL.304 {ECO:0000312|EMBL:CAB78590.1};
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].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) 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).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12721858; DOI=10.1007/s00425-002-0969-0;
RA Messner B., Thulke O., Schaeffner A.R.;
RT "Arabidopsis glucosyltransferases with activities toward both endogenous
RT and xenobiotic substrates.";
RL Planta 217:138-146(2003).
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). Can glucosylate the phytotoxic xenobiotic compound
CC 2,4,5-trichlorophenol (TCP) (PubMed:12721858).
CC {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:11187886,
CC ECO:0000269|PubMed:12721858}.
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=400 uM for 4-coumarate {ECO:0000269|PubMed:11042211};
CC KM=340 uM for ferulate {ECO:0000269|PubMed:11042211};
CC KM=180 uM for caffeate {ECO:0000269|PubMed:11042211};
CC KM=580 uM for sinapate {ECO:0000269|PubMed:11042211};
CC KM=710 uM for cinnamate {ECO:0000269|PubMed:11042211};
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers and siliques.
CC {ECO:0000269|PubMed:12721858}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10326.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB78590.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z97339; CAB10326.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161541; CAB78590.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE83609.1; -; Genomic_DNA.
DR EMBL; BT002014; AAN72025.1; -; mRNA.
DR EMBL; BT015796; AAU93568.1; -; mRNA.
DR PIR; D71419; D71419.
DR RefSeq; NP_193283.2; NM_117638.3.
DR AlphaFoldDB; Q5XF20; -.
DR SMR; Q5XF20; -.
DR STRING; 3702.AT4G15480.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q5XF20; -.
DR PRIDE; Q5XF20; -.
DR ProteomicsDB; 228588; -.
DR EnsemblPlants; AT4G15480.1; AT4G15480.1; AT4G15480.
DR GeneID; 827220; -.
DR Gramene; AT4G15480.1; AT4G15480.1; AT4G15480.
DR KEGG; ath:AT4G15480; -.
DR Araport; AT4G15480; -.
DR TAIR; locus:2130205; AT4G15480.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; Q5XF20; -.
DR OMA; MGSISEM; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q5XF20; -.
DR BioCyc; ARA:AT4G15480-MON; -.
DR SABIO-RK; Q5XF20; -.
DR PRO; PR:Q5XF20; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5XF20; baseline and differential.
DR Genevisible; Q5XF20; 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 GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR GO; GO:0010224; P:response to UV-B; IGI: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 Detoxification; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..490
FT /note="UDP-glycosyltransferase 84A1"
FT /id="PRO_0000409120"
FT BINDING 296
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 356..358
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 373..381
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 395..398
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT CONFLICT 237
FT /note="Q -> R (in Ref. 4; AAN72025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54481 MW; 2641C4C1C13AC302 CRC64;
MGSISEMVFE TCPSPNPIHV MLVSFQGQGH VNPLLRLGKL IASKGLLVTF VTTELWGKKM
RQANKIVDGE LKPVGSGSIR FEFFDEEWAE DDDRRADFSL YIAHLESVGI REVSKLVRRY
EEANEPVSCL INNPFIPWVC HVAEEFNIPC AVLWVQSCAC FSAYYHYQDG SVSFPTETEP
ELDVKLPCVP VLKNDEIPSF LHPSSRFTGF RQAILGQFKN LSKSFCVLID SFDSLEQEVI
DYMSSLCPVK TVGPLFKVAR TVTSDVSGDI CKSTDKCLEW LDSRPKSSVV YISFGTVAYL
KQEQIEEIAH GVLKSGLSFL WVIRPPPHDL KVETHVLPQE LKESSAKGKG MIVDWCPQEQ
VLSHPSVACF VTHCGWNSTM ESLSSGVPVV CCPQWGDQVT DAVYLIDVFK TGVRLGRGAT
EERVVPREEV AEKLLEATVG EKAEELRKNA LKWKAEAEAA VAPGGSSDKN FREFVEKLGA
GVTKTKDNGY
