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Q9LSY9 (U71B1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glycosyltransferase 71B1

EC=2.4.1.-
Alternative name(s):
Flavonol 3-O-glucosyltransferase UGT71B1
EC=2.4.1.91
Gene names
Name:UGT71B1
Ordered Locus Names:At3g21750
ORF Names:MSD21.6, MSD21.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Possesses quercetin 3-O-glucosyltransferase activity in vitro. Also active in vitro on benzoates and benzoate derivatives. Ref.6 Ref.7

Catalytic activity

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

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Sequence caution

The sequence AAK32764.1 differs from that shown. Reason: Frameshift at position 455.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473UDP-glycosyltransferase 71B1
PRO_0000409047

Regions

Region342 – 3443UDP-glucose binding By similarity
Region359 – 3679UDP-glucose binding By similarity
Region381 – 3844UDP-glucose binding By similarity

Sites

Binding site2731UDP-glucose By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LSY9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 42B7925984C350B0

FASTA47352,666
        10         20         30         40         50         60 
MKVELVFIPS PGVGHIRATT ALAKLLVASD NRLSVTLIVI PSRVSDDASS SVYTNSEDRL 

        70         80         90        100        110        120 
RYILLPARDQ TTDLVSYIDS QKPQVRAVVS KVAGDVSTRS DSRLAGIVVD MFCTSMIDIA 

       130        140        150        160        170        180 
DEFNLSAYIF YTSNASYLGL QFHVQSLYDE KELDVSEFKD TEMKFDVPTL TQPFPAKCLP 

       190        200        210        220        230        240 
SVMLNKKWFP YVLGRARSFR ATKGILVNSV ADMEPQALSF FSGGNGNTNI PPVYAVGPIM 

       250        260        270        280        290        300 
DLESSGDEEK RKEILHWLKE QPTKSVVFLC FGSMGGFSEE QAREIAVALE RSGHRFLWSL 

       310        320        330        340        350        360 
RRASPVGNKS NPPPGEFTNL EEILPKGFLD RTVEIGKIIS WAPQVDVLNS PAIGAFVTHC 

       370        380        390        400        410        420 
GWNSILESLW FGVPMAAWPI YAEQQFNAFH MVDELGLAAE VKKEYRRDFL VEEPEIVTAD 

       430        440        450        460        470 
EIERGIKCAM EQDSKMRKRV MEMKDKLHVA LVDGGSSNCA LKKFVQDVVD NVP 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [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. expand/collapse author list , 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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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.
[6]"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.
[7]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025634 Genomic DNA. Translation: BAB02837.1.
CP002686 Genomic DNA. Translation: AEE76548.1.
AF361596 mRNA. Translation: AAK32764.1. Frameshift.
AK227147 mRNA. Translation: BAE99192.1.
RefSeqNP_188812.1. NM_113070.2.
UniGeneAt.19110.
At.66536.

3D structure databases

ProteinModelPortalQ9LSY9.
SMRQ9LSY9. Positions 4-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G21750.1-P.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

Proteomic databases

PaxDbQ9LSY9.
PRIDEQ9LSY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G21750.1; AT3G21750.1; AT3G21750.
GeneID821729.
KEGGath:AT3G21750.

Organism-specific databases

TAIRAT3G21750.

Phylogenomic databases

eggNOGKOG1192.
HOGENOMHOG000237568.
InParanoidQ9LSY9.
OMAGHIRATT.
PhylomeDBQ9LSY9.
ProtClustDBPLN02554.

Enzyme and pathway databases

BioCycARA:AT3G21750-MONOMER.
MetaCyc:AT3G21750-MONOMER.

Gene expression databases

GenevestigatorQ9LSY9.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERPTHR11926. PTHR11926. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameU71B1_ARATH
AccessionPrimary (citable) accession number: Q9LSY9
Secondary accession number(s): Q9ASY6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names