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   27-MAR-2024, entry version 120.
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.Q8W491; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; 3702-AT4G34131-1; -.
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; AT4G34131; UGT73B3.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_2_2_1; -.
DR   InParanoid; Q8W491; -.
DR   OMA; TIEFPCA; -.
DR   OrthoDB; 1208220at2759; -.
DR   PhylomeDB; Q8W491; -.
DR   PRO; PR:Q8W491; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8W491; baseline and differential.
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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48047; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48047:SF45; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
DR   Genevisible; Q8W491; AT.
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   ACT_SITE        21
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   ACT_SITE        132
FT                   /note="Charge relay"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         21
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         355
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         357
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         372
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         375
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         376
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         377
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         380
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         395
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         396
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         397
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
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
//