U73B2_ARATH
ID U73B2_ARATH Reviewed; 483 AA.
AC Q94C57;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=UDP-glucosyl transferase 73B2;
DE EC=2.4.1.-;
DE AltName: Full=Flavonol 7-O-glucosyltransferase;
DE EC=2.4.1.237 {ECO:0000269|PubMed:14697269};
DE AltName: Full=UDP glucose:flavonoid 7-O-glucosyltransferase;
GN Name=UGT73B2; OrderedLocusNames=At4g34135; ORFNames=F28A23;
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Leaf;
RX PubMed=14697269; DOI=10.1016/j.phytochem.2003.10.005;
RA Willits M.G., Giovanni M., Prata R.T., Kramer C.M., De Luca V.,
RA Steffens J.C., Graser G.;
RT "Bio-fermentation of modified flavonoids: an example of in vivo
RT diversification of secondary metabolites.";
RL Phytochemistry 65:31-41(2004).
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 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 [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 TISSUE SPECIFICITY, AND INDUCTION BY 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: Catalyzes the glycosylation of flavonoids from UDP-glucose.
CC Uses a wide range of flavonoid substrates including flavonols
CC (quercetin, kaempferol, isorhamnetin, 3-OH 7,2',4'-MeO-flavone),
CC flavones (luteolin, apigenin), flavanones (naringenin, hesperetin),
CC flavanonols (taxifolin), isoflavones (genistein, daidzein), flavonol
CC glycosides (quercitrin, isoquercitrin, rutin), and chalcones
CC (isoliquiritigenin). Specific for the C-7 position, with a 20-fold
CC lower activity for the C-3 position. {ECO:0000269|PubMed:14697269,
CC ECO:0000269|PubMed:15352060}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 7-O-hydroxy-flavonol + UDP-alpha-D-glucose = a flavonol 7-O-
CC beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:23164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:52144, ChEBI:CHEBI:52267,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.237;
CC Evidence={ECO:0000269|PubMed:14697269};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94C57-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:16306146}.
CC -!- INDUCTION: Not induced by salicylic acid.
CC {ECO:0000269|PubMed:16306146}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY339370; AAR01231.1; -; mRNA.
DR EMBL; AL161584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE86328.1; -; Genomic_DNA.
DR EMBL; AY035164; AAK59668.1; -; mRNA.
DR EMBL; AY142692; AAN13230.1; -; mRNA.
DR RefSeq; NP_567954.1; NM_119575.2. [Q94C57-1]
DR AlphaFoldDB; Q94C57; -.
DR SMR; Q94C57; -.
DR STRING; 3702.AT4G34135.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q94C57; -.
DR PRIDE; Q94C57; -.
DR ProteomicsDB; 228729; -. [Q94C57-1]
DR EnsemblPlants; AT4G34135.1; AT4G34135.1; AT4G34135. [Q94C57-1]
DR GeneID; 829560; -.
DR Gramene; AT4G34135.1; AT4G34135.1; AT4G34135. [Q94C57-1]
DR KEGG; ath:AT4G34135; -.
DR Araport; AT4G34135; -.
DR TAIR; locus:505006555; AT4G34135.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_2_2_1; -.
DR InParanoid; Q94C57; -.
DR OMA; FCELEPD; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q94C57; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q94C57; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94C57; baseline and differential.
DR Genevisible; Q94C57; AT.
DR GO; GO:0047893; F:flavonol 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0033836; F:flavonol 7-O-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0051555; P:flavonol biosynthetic process; IDA:TAIR.
DR GO; GO:0051707; P:response to other organism; IEP: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 Alternative splicing; Flavonoid biosynthesis; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..483
FT /note="UDP-glucosyl transferase 73B2"
FT /id="PRO_0000403934"
FT BINDING 298
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 483 AA; 54215 MW; 764C04794420658C CRC64;
MGSDHHHRKL HVMFFPFMAY GHMIPTLDMA KLFSSRGAKS TILTTSLNSK ILQKPIDTFK
NLNPGLEIDI QIFNFPCVEL GLPEGCENVD FFTSNNNDDK NEMIVKFFFS TRFFKDQLEK
LLGTTRPDCL IADMFFPWAT EAAGKFNVPR LVFHGTGYFS LCAGYCIGVH KPQKRVASSS
EPFVIPELPG NIVITEEQII DGDGESDMGK FMTEVRESEV KSSGVVLNSF YELEHDYADF
YKSCVQKRAW HIGPLSVYNR GFEEKAERGK KANIDEAECL KWLDSKKPNS VIYVSFGSVA
FFKNEQLFEI AAGLEASGTS FIWVVRKTKD DREEWLPEGF EERVKGKGMI IRGWAPQVLI
LDHQATGGFV THCGWNSLLE GVAAGLPMVT WPVGAEQFYN EKLVTQVLRT GVSVGASKHM
KVMMGDFISR EKVDKAVREV LAGEAAEERR RRAKKLAAMA KAAVEEGGSS FNDLNSFMEE
FSS
