ID   UFOG6_FRAAN             Reviewed;         479 AA.
AC   Q2V6K0;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=UDP-glucose flavonoid 3-O-glucosyltransferase 6 {ECO:0000303|PubMed:18487633};
DE            EC=2.4.1.91 {ECO:0000269|PubMed:18487633};
DE   AltName: Full=Flavonol 3-O-glucosyltransferase 6 {ECO:0000303|PubMed:18487633};
DE            Short=FaGT6 {ECO:0000303|PubMed:18487633};
GN   Name=GT6 {ECO:0000312|EMBL:ABB92748.1};
OS   Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC   Fragaria.
OX   NCBI_TaxID=3747;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABB92748.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   STRAIN=cv. Elsanta {ECO:0000269|PubMed:18487633};
RC   TISSUE=Fruit {ECO:0000269|PubMed:18487633};
RX   PubMed=18487633; DOI=10.1093/jxb/ern117;
RA   Griesser M., Vitzthum F., Fink B., Bellido M.L., Raasch C.,
RA   Munoz-Blanco J., Schwab W.;
RT   "Multi-substrate flavonol O-glucosyltransferases from strawberry (Fragaria
RT   x ananassa) achene and receptacle.";
RL   J. Exp. Bot. 59:2611-2625(2008).
CC   -!- FUNCTION: Broad spectrum multifunctional glucosyltransferase. Catalyzes
CC       the formation of flavonol 3-O-glucosides during fruit ripening.
CC       Accepted substrates include several flavonoids, hydroxycoumarins and
CC       beta-naphthols. Uses UDP-Glc as a sugar donor, but not UDP-Gal or UDP-
CC       GlcUA. May also be involved in detoxification of xenobiotics.
CC       {ECO:0000269|PubMed:18487633}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-
CC         glucoside + H(+) + UDP; Xref=Rhea:RHEA:22300, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16816, ChEBI:CHEBI:28802, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.91;
CC         Evidence={ECO:0000269|PubMed:18487633};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.3 uM for 3-hydroxyflavone {ECO:0000269|PubMed:18487633};
CC         KM=2.0 mM for UDP-glucose {ECO:0000269|PubMed:18487633};
CC         Vmax=1.4 nmol/sec/mg enzyme with 3-hydroxyflavone as substrate
CC         {ECO:0000269|PubMed:18487633};
CC         Vmax=0.5 nmol/sec/mg enzyme with UDP-glucose as substrate
CC         {ECO:0000269|PubMed:18487633};
CC         Note=The kinetic constants are determined for the recombinant GST-
CC         fusion protein. {ECO:0000269|PubMed:18487633};
CC       pH dependence:
CC         Optimum pH is 7.5-8. {ECO:0000269|PubMed:18487633};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:18487633};
CC   -!- TISSUE SPECIFICITY: Strongly expressed in achenes, with lower
CC       expression levels detected in receptacles.
CC       {ECO:0000269|PubMed:18487633}.
CC   -!- DEVELOPMENTAL STAGE: The expression in receptacles is ripening-related,
CC       with highest expression detected in red fruit.
CC       {ECO:0000269|PubMed:18487633}.
CC   -!- INDUCTION: By de-achening. By injection with salicylic acid, with
CC       transcript levels increasing by a factor of 5-6 at 4 hours post-
CC       injection, remaining stable until 6 hours post-injection and falling
CC       below control levels at 8 hours post-injection. Down-regulated by
CC       synthetic auxin naphthaleneacetic acid (NAA).
CC       {ECO:0000269|PubMed:18487633}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ289587; ABB92748.1; -; mRNA.
DR   AlphaFoldDB; Q2V6K0; -.
DR   SMR; Q2V6K0; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   BioCyc; MetaCyc:MON-17433; -.
DR   GO; GO:0102360; F:daphnetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047893; F:flavonol 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102425; F:myricetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
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   Glycosyltransferase; Transferase.
FT   CHAIN           1..479
FT                   /note="UDP-glucose flavonoid 3-O-glucosyltransferase 6"
FT                   /id="PRO_0000413769"
FT   REGION          454..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  53477 MW;  F7E4BAD1CB8D14D4 CRC64;
     MKKASELIFI PIPGIGHIVS TVEIAKLLLC RDDNLFITIL IMKFPFTADG SDVYIKSLAV
     DPSLKTQRIR FVNLPQEHFQ GTGATGFFTF IDSHKSHVKD AVTRLMETKS ETTRIAGFVI
     DMFCTGMIDL ANEFGLPSYV FYTSGAADLG LMFHLQALRD EENKDCTEFK DSDAELVVSS
     FVNPLPAARV LPSVVFEKEG GNFFLNFAKR YRETKGILVN TFLELEPHAI QSLSSDGKIL
     PVYPVGPILN VKSEGNQVSS EKSKQKSDIL EWLDDQPPSS VVFLCFGSMG CFGEDQVKEI
     AHALEQGGIR FLWSLRQPSK EKIGFPSDYT DYKAVLPEGF LDRTTDLGKV IGWAPQLAIL
     AHPAVGGFVS HCGWNSTLES IWYGVPIATW PFYAEQQVNA FELVKELKLA VEIDMGYRKD
     SGVIVSRENI EKGIKEVMEQ ESELRKRVKE MSQMSRKALE EDGSSYSSLG RFLDQIQTS