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Protein

UDP-glucose flavonoid 3-O-glucosyltransferase 6

Gene

GT6

Organism
Fragaria ananassa (Strawberry)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Broad spectrum multifunctional glucosyltransferase. Catalyzes the formation of flavonol 3-O-glucosides during fruit ripening. Accepted substrates include several flavonoids, hydroxycoumarins and beta-naphthols. Uses UDP-Glc as a sugar donor, but not UDP-Gal or UDP-GlcUA. May also be involved in detoxification of xenobiotics.1 Publication

Catalytic activityi

UDP-glucose + a flavonol = UDP + a flavonol 3-O-D-glucoside.1 Publication

Kineticsi

The kinetic constants are determined for the recombinant GST-fusion protein.1 Publication

  1. KM=5.3 µM for 3-hydroxyflavone1 Publication
  2. KM=2.0 mM for UDP-glucose1 Publication
  1. Vmax=1.4 nmol/sec/mg enzyme with 3-hydroxyflavone as substrate1 Publication
  2. Vmax=0.5 nmol/sec/mg enzyme with UDP-glucose as substrate1 Publication

pH dependencei

Optimum pH is 7.5-8.1 Publication

Temperature dependencei

Optimum temperature is 35 degrees Celsius.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17433.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose flavonoid 3-O-glucosyltransferase 61 Publication (EC:2.4.1.911 Publication)
Alternative name(s):
Flavonol 3-O-glucosyltransferase 61 Publication
Short name:
FaGT61 Publication
Gene namesi
Name:GT6Imported
OrganismiFragaria ananassa (Strawberry)
Taxonomic identifieri3747 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeRosoideaePotentilleaeFragariinaeFragaria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479UDP-glucose flavonoid 3-O-glucosyltransferase 6PRO_0000413769Add
BLAST

Expressioni

Tissue specificityi

Strongly expressed in achenes, with lower expression levels detected in receptacles.1 Publication

Developmental stagei

The expression in receptacles is ripening-related, with highest expression detected in red fruit.1 Publication

Inductioni

By de-achening. By injection with salicylic acid, with transcript levels increasing by a factor of 5-6 at 4 hours post-injection, remaining stable until 6 hours post-injection and falling below control levels at 8 hours post-injection. Down-regulated by synthetic auxin naphthaleneacetic acid (NAA).1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ2V6K0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Sequence Analysis

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.

Q2V6K0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKASELIFI PIPGIGHIVS TVEIAKLLLC RDDNLFITIL IMKFPFTADG
60 70 80 90 100
SDVYIKSLAV DPSLKTQRIR FVNLPQEHFQ GTGATGFFTF IDSHKSHVKD
110 120 130 140 150
AVTRLMETKS ETTRIAGFVI DMFCTGMIDL ANEFGLPSYV FYTSGAADLG
160 170 180 190 200
LMFHLQALRD EENKDCTEFK DSDAELVVSS FVNPLPAARV LPSVVFEKEG
210 220 230 240 250
GNFFLNFAKR YRETKGILVN TFLELEPHAI QSLSSDGKIL PVYPVGPILN
260 270 280 290 300
VKSEGNQVSS EKSKQKSDIL EWLDDQPPSS VVFLCFGSMG CFGEDQVKEI
310 320 330 340 350
AHALEQGGIR FLWSLRQPSK EKIGFPSDYT DYKAVLPEGF LDRTTDLGKV
360 370 380 390 400
IGWAPQLAIL AHPAVGGFVS HCGWNSTLES IWYGVPIATW PFYAEQQVNA
410 420 430 440 450
FELVKELKLA VEIDMGYRKD SGVIVSRENI EKGIKEVMEQ ESELRKRVKE
460 470
MSQMSRKALE EDGSSYSSLG RFLDQIQTS
Length:479
Mass (Da):53,477
Last modified:January 10, 2006 - v1
Checksum:iF7E4BAD1CB8D14D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ289587 mRNA. Translation: ABB92748.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ289587 mRNA. Translation: ABB92748.1.

3D structure databases

ProteinModelPortaliQ2V6K0.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17433.

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

  1. "Multi-substrate flavonol O-glucosyltransferases from strawberry (Fragaria x ananassa) achene and receptacle."
    Griesser M., Vitzthum F., Fink B., Bellido M.L., Raasch C., Munoz-Blanco J., Schwab W.
    J. Exp. Bot. 59:2611-2625(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: cv. Elsanta1 Publication.
    Tissue: Fruit1 Publication.

Entry informationi

Entry nameiUFOG6_FRAAN
AccessioniPrimary (citable) accession number: Q2V6K0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: January 10, 2006
Last modified: May 27, 2015
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. 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.