U84A4_ARATH
ID U84A4_ARATH Reviewed; 475 AA.
AC O23402;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=UDP-glycosyltransferase 84A4 {ECO:0000303|PubMed:11042215};
DE EC=2.4.1.120 {ECO:0000269|PubMed:11187886};
DE EC=2.4.1.177 {ECO:0000269|PubMed:11187886};
DE AltName: Full=Hydroxycinnamate glucosyltransferase 1 {ECO:0000303|PubMed:11187886};
DE Short=AtHCAGT1 {ECO:0000303|PubMed:11187886};
GN Name=UGT84A4 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At4g15500 {ECO:0000312|Araport:AT4G15500};
GN ORFNames=dl3790c {ECO:0000312|EMBL:CAB10328.1},
GN FCAALL.307 {ECO:0000312|EMBL:CAB78592.1};
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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).
CC -!- FUNCTION: UDP-glucosyltransferase that forms glucose esters with
CC phenylpropanoids (PubMed:11187886). Glucosylates 4-coumarate, ferulate,
CC caffeate, sinapate and cinnamate (PubMed:11187886).
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: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: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: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: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:11187886};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z97339; CAB10328.1; -; Genomic_DNA.
DR EMBL; AL161541; CAB78592.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83611.1; -; Genomic_DNA.
DR EMBL; BT012573; AAS99717.1; -; mRNA.
DR EMBL; AK229801; BAF01632.1; -; mRNA.
DR PIR; F71419; F71419.
DR RefSeq; NP_193285.1; NM_117640.4.
DR AlphaFoldDB; O23402; -.
DR SMR; O23402; -.
DR STRING; 3702.AT4G15500.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; O23402; -.
DR PRIDE; O23402; -.
DR ProteomicsDB; 242592; -.
DR EnsemblPlants; AT4G15500.1; AT4G15500.1; AT4G15500.
DR GeneID; 827222; -.
DR Gramene; AT4G15500.1; AT4G15500.1; AT4G15500.
DR KEGG; ath:AT4G15500; -.
DR Araport; AT4G15500; -.
DR TAIR; locus:2130225; AT4G15500.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; O23402; -.
DR OMA; DECTAWL; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; O23402; -.
DR BioCyc; ARA:AT4G15500-MON; -.
DR BRENDA; 2.4.1.126; 399.
DR PRO; PR:O23402; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23402; baseline and differential.
DR Genevisible; O23402; 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..475
FT /note="UDP-glycosyltransferase 84A4"
FT /id="PRO_0000409123"
FT BINDING 285
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 340..342
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 357..365
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 379..382
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 53496 MW; 339E81BA5BAD55FC CRC64;
MEMESSLPHV MLVSFPGQGH ISPLLRLGKI IASKGLIVTF VTTEEPLGKK MRQANNIQDG
VLKPVGLGFL RFEFFEDGFV YKEDFDLLQK SLEVSGKREI KNLVKKYEKQ PVRCLINNAF
VPWVCDIAEE LQIPSAVLWV QSCACLAAYY YYHHQLVKFP TETEPEITVD VPFKPLTLKH
DEIPSFLHPS SPLSSIGGTI LEQIKRLHKP FSVLIETFQE LEKDTIDHMS QLCPQVNFNP
IGPLFTMAKT IRSDIKGDIS KPDSDCIEWL DSREPSSVVY ISFGTLAFLK QNQIDEIAHG
ILNSGLSCLW VLRPPLEGLA IEPHVLPLEL EEKGKIVEWC QQEKVLAHPA VACFLSHCGW
NSTMEALTSG VPVICFPQWG DQVTNAVYMI DVFKTGLRLS RGASDERIVP REEVAERLLE
ATVGEKAVEL RENARRWKEE AESAVAYGGT SERNFQEFVD KLVDVKTMTN INNVV
