U73B3_ARATH
ID U73B3_ARATH Reviewed; 481 AA.
AC Q8W491;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=UDP-glycosyltransferase 73B3;
DE EC=2.4.1.-;
DE AltName: Full=Flavonol 3-O-glucosyltransferase UGT73B3;
DE EC=2.4.1.91;
GN Name=UGT73B3; OrderedLocusNames=At4g34131; ORFNames=F28A23.120;
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=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 [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.
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, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP PATHOGEN AND SALICYLIC ACID.
RX PubMed=16306146; DOI=10.1104/pp.105.067223;
RA Langlois-Meurinne M., Gachon C.M., Saindrenan P.;
RT "Pathogen-responsive expression of glycosyltransferase genes UGT73B3 and
RT UGT73B5 is necessary for resistance to Pseudomonas syringae pv tomato in
RT Arabidopsis.";
RL Plant Physiol. 139:1890-1901(2005).
CC -!- FUNCTION: Possesses quercetin 3-O-glucosyltransferase activity in
CC vitro. Also active in vitro on benzoates and benzoate derivatives.
CC Involved in stress or defense responses. {ECO:0000269|PubMed:11641410,
CC ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:16306146}.
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 -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:16306146}.
CC -!- INDUCTION: Induced by pathogen infection, by H(2)O(2) and by salicylic
CC acid. {ECO:0000269|PubMed:16306146}.
CC -!- DISRUPTION PHENOTYPE: Decreased resistance to avirulent strains of
CC P.syringae. {ECO:0000269|PubMed:16306146}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL161584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE86327.1; -; Genomic_DNA.
DR EMBL; AY062753; AAL32831.1; -; mRNA.
DR EMBL; AY114680; AAM47999.1; -; mRNA.
DR RefSeq; NP_567953.1; NM_119574.3.
DR AlphaFoldDB; Q8W491; -.
DR SMR; Q8W491; -.
DR STRING; 3702.AT4G34131.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q8W491; -.
DR PRIDE; Q8W491; -.
DR ProteomicsDB; 228558; -.
DR EnsemblPlants; AT4G34131.1; AT4G34131.1; AT4G34131.
DR GeneID; 829559; -.
DR Gramene; AT4G34131.1; AT4G34131.1; AT4G34131.
DR KEGG; ath:AT4G34131; -.
DR Araport; AT4G34131; -.
DR TAIR; locus:2831352; AT4G34131.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_2_2_1; -.
DR InParanoid; Q8W491; -.
DR OMA; GVQTWIG; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q8W491; -.
DR PRO; PR:Q8W491; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W491; baseline and differential.
DR Genevisible; Q8W491; AT.
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:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IMP: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 2: Evidence at transcript level;
KW Glycosyltransferase; Plant defense; Reference proteome; Transferase.
FT CHAIN 1..481
FT /note="UDP-glycosyltransferase 73B3"
FT /id="PRO_0000403936"
FT BINDING 297
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 355..357
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 372..380
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 394..397
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 54591 MW; FAE0484361DD072A CRC64;
MSSDPHRKLH VVFFPFMAYG HMIPTLDMAK LFSSRGAKST ILTTPLNSKI FQKPIERFKN
LNPSFEIDIQ IFDFPCVDLG LPEGCENVDF FTSNNNDDRQ YLTLKFFKST RFFKDQLEKL
LETTRPDCLI ADMFFPWATE AAEKFNVPRL VFHGTGYFSL CSEYCIRVHN PQNIVASRYE
PFVIPDLPGN IVITQEQIAD RDEESEMGKF MIEVKESDVK SSGVIVNSFY ELEPDYADFY
KSVVLKRAWH IGPLSVYNRG FEEKAERGKK ASINEVECLK WLDSKKPDSV IYISFGSVAC
FKNEQLFEIA AGLETSGANF IWVVRKNIGI EKEEWLPEGF EERVKGKGMI IRGWAPQVLI
LDHQATCGFV THCGWNSLLE GVAAGLPMVT WPVAAEQFYN EKLVTQVLRT GVSVGAKKNV
RTTGDFISRE KVVKAVREVL VGEEADERRE RAKKLAEMAK AAVEGGSSFN DLNSFIEEFT
S
