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Q2V6J9 (UFOG7_FRAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-glucose flavonoid 3-O-glucosyltransferase 7

EC=2.4.1.91
Alternative name(s):
Flavonol 3-O-glucosyltransferase 7
Short name=FaGT7
Gene names
Name:GT7
OrganismFragaria ananassa (Strawberry)
Taxonomic identifier3747 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeRosoideaePotentilleaeFragariinaeFragaria

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Broad spectrum multifunctional glucosyltransferase. Catalyzes the formation of flavonol 3-O- and 4'-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. Ref.1

Catalytic activity

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

Tissue specificity

Strongly expressed in achenes and receptacles. Ref.1

Developmental stage

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

Induction

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). Ref.1

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=3.5 µM for isorhamnetin Ref.1

KM=0.6 mM for UDP-glucose Ref.1

Vmax=2.8 nmol/sec/mg enzyme with isorhamnetin as substrate Ref.1

Vmax=2.7 nmol/sec/mg enzyme with UDP-glucose as substrate Ref.1

pH dependence:

Optimum pH is 6.5. Ref.1

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Ref.1

Ontologies

Keywords
   Molecular functionGlycosyltransferase
Transferase
Gene Ontology (GO)
   Molecular_functionflavonol 3-O-glucosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487UDP-glucose flavonoid 3-O-glucosyltransferase 7
PRO_0000413770

Sequences

Sequence LengthMass (Da)Tools
Q2V6J9 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 313E7EB3889985FD

FASTA48754,652
        10         20         30         40         50         60 
MAMETKSCQQ LHIFFLPFMA RGHSIPLTDI AKLFSSHGAR CTIVTTPLNA PLFSKATQRG 

        70         80         90        100        110        120 
EIELVLIKFP SAEAGLPQDC ESADLITTQD MLGKFVKATF LIEPHFEKIL DEHRPHCLVA 

       130        140        150        160        170        180 
DAFFTWATDV AAKFRIPRLY FHGTGFFALC ASLSVMMYQP HSNLSSDSES FVIPNLPDEI 

       190        200        210        220        230        240 
KMTRSQLPVF PDESEFMKML KASIEIEERS YGVIVNSFYE LEPAYANHYR KVFGRKAWHI 

       250        260        270        280        290        300 
GPVSFCNKAI EDKAERGSIK SSTAEKHECL KWLDSKKPRS VVYVSFGSMV RFADSQLLEI 

       310        320        330        340        350        360 
ATGLEASGQD FIWVVKKEKK EVEEWLPEGF EKRMEGKGLI IRDWAPQVLI LEHEAIGAFV 

       370        380        390        400        410        420 
THCGWNSILE AVSAGVPMIT WPVFGEQFYN EKLVTEIHRI GVPVGSEKWA LSFVDVNAET 

       430        440        450        460        470        480 
EGRVRREAIE EAVTRIMVGD EAVETRSRVK ELGENARRAV EEGGSSFLDL SALVGELNDL 


AFGGLVE 

« Hide

References

[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. Elsanta.
Tissue: Fruit.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ289588 mRNA. Translation: ABB92749.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameUFOG7_FRAAN
AccessionPrimary (citable) accession number: Q2V6J9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: January 10, 2006
Last modified: February 19, 2014
This is version 27 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