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Protein

UDP-glycosyltransferase 73B3

Gene

UGT73B3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Possesses quercetin 3-O-glucosyltransferase activity in vitro. Also active in vitro on benzoates and benzoate derivatives. Involved in stress or defense responses.3 Publications

Catalytic activityi

UDP-glucose + a flavonol = UDP + a flavonol 3-O-D-glucoside.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei297 – 2971UDP-glucoseBy similarity

GO - Molecular functioni

  1. flavonol 3-O-glucosyltransferase activity Source: UniProtKB-EC
  2. quercetin 3-O-glucosyltransferase activity Source: TAIR
  3. quercetin 7-O-glucosyltransferase activity Source: GO_Central
  4. UDP-glucosyltransferase activity Source: TAIR

GO - Biological processi

  1. defense response Source: UniProtKB-KW
  2. flavonoid biosynthetic process Source: GO_Central
  3. flavonoid glucuronidation Source: GO_Central
  4. response to other organism Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Plant defense

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glycosyltransferase 73B3 (EC:2.4.1.-)
Alternative name(s):
Flavonol 3-O-glucosyltransferase UGT73B3 (EC:2.4.1.91)
Gene namesi
Name:UGT73B3
Ordered Locus Names:At4g34131
ORF Names:F28A23.120
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G34131.

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Decreased resistance to avirulent strains of P.syringae.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481UDP-glycosyltransferase 73B3PRO_0000403936Add
BLAST

Proteomic databases

PaxDbiQ8W491.
PRIDEiQ8W491.

Expressioni

Tissue specificityi

Expressed in roots and flowers.1 Publication

Inductioni

Induced by pathogen infection, by H2O2 and by salicylic acid.1 Publication

Gene expression databases

GenevestigatoriQ8W491.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G34131.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8W491.
SMRiQ8W491. Positions 9-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni355 – 3573UDP-glucose bindingBy similarity
Regioni372 – 3809UDP-glucose bindingBy similarity
Regioni394 – 3974UDP-glucose bindingBy similarity

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Phylogenomic databases

eggNOGiNOG263906.
HOGENOMiHOG000237565.
InParanoidiQ8W491.
OMAiETSGANF.
PhylomeDBiQ8W491.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8W491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDPHRKLH VVFFPFMAYG HMIPTLDMAK LFSSRGAKST ILTTPLNSKI
60 70 80 90 100
FQKPIERFKN LNPSFEIDIQ IFDFPCVDLG LPEGCENVDF FTSNNNDDRQ
110 120 130 140 150
YLTLKFFKST RFFKDQLEKL LETTRPDCLI ADMFFPWATE AAEKFNVPRL
160 170 180 190 200
VFHGTGYFSL CSEYCIRVHN PQNIVASRYE PFVIPDLPGN IVITQEQIAD
210 220 230 240 250
RDEESEMGKF MIEVKESDVK SSGVIVNSFY ELEPDYADFY KSVVLKRAWH
260 270 280 290 300
IGPLSVYNRG FEEKAERGKK ASINEVECLK WLDSKKPDSV IYISFGSVAC
310 320 330 340 350
FKNEQLFEIA AGLETSGANF IWVVRKNIGI EKEEWLPEGF EERVKGKGMI
360 370 380 390 400
IRGWAPQVLI LDHQATCGFV THCGWNSLLE GVAAGLPMVT WPVAAEQFYN
410 420 430 440 450
EKLVTQVLRT GVSVGAKKNV RTTGDFISRE KVVKAVREVL VGEEADERRE
460 470 480
RAKKLAEMAK AAVEGGSSFN DLNSFIEEFT S
Length:481
Mass (Da):54,591
Last modified:March 1, 2002 - v1
Checksum:iFAE0484361DD072A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161584 Genomic DNA. No translation available.
CP002687 Genomic DNA. Translation: AEE86327.1.
AY062753 mRNA. Translation: AAL32831.1.
AY114680 mRNA. Translation: AAM47999.1.
RefSeqiNP_567953.1. NM_119574.3.
UniGeneiAt.27243.
At.68482.

Genome annotation databases

EnsemblPlantsiAT4G34131.1; AT4G34131.1; AT4G34131.
GeneIDi829559.
KEGGiath:AT4G34131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161584 Genomic DNA. No translation available.
CP002687 Genomic DNA. Translation: AEE86327.1.
AY062753 mRNA. Translation: AAL32831.1.
AY114680 mRNA. Translation: AAM47999.1.
RefSeqiNP_567953.1. NM_119574.3.
UniGeneiAt.27243.
At.68482.

3D structure databases

ProteinModelPortaliQ8W491.
SMRiQ8W491. Positions 9-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G34131.1-P.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Proteomic databases

PaxDbiQ8W491.
PRIDEiQ8W491.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G34131.1; AT4G34131.1; AT4G34131.
GeneIDi829559.
KEGGiath:AT4G34131.

Organism-specific databases

TAIRiAT4G34131.

Phylogenomic databases

eggNOGiNOG263906.
HOGENOMiHOG000237565.
InParanoidiQ8W491.
OMAiETSGANF.
PhylomeDBiQ8W491.

Gene expression databases

GenevestigatoriQ8W491.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of Arabidopsis thaliana."
    Li Y., Baldauf S., Lim E.K., Bowles D.J.
    J. Biol. Chem. 276:4338-4343(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  5. "The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-hydroxybenzoic acid, and other benzoates."
    Lim E.K., Doucet C.J., Li Y., Elias L., Worrall D., Spencer S.P., Ross J., Bowles D.J.
    J. Biol. Chem. 277:586-592(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Arabidopsis glycosyltransferases as biocatalysts in fermentation for regioselective synthesis of diverse quercetin glucosides."
    Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.
    Biotechnol. Bioeng. 87:623-631(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Pathogen-responsive expression of glycosyltransferase genes UGT73B3 and UGT73B5 is necessary for resistance to Pseudomonas syringae pv tomato in Arabidopsis."
    Langlois-Meurinne M., Gachon C.M., Saindrenan P.
    Plant Physiol. 139:1890-1901(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INDUCTION BY PATHOGEN AND SALICYLIC ACID.

Entry informationi

Entry nameiU73B3_ARATH
AccessioniPrimary (citable) accession number: Q8W491
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: March 1, 2002
Last modified: February 4, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.