ID   UFOG7_FRAAN             Reviewed;         487 AA.
AC   Q2V6J9;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   22-FEB-2023, entry version 46.
DE   RecName: Full=UDP-glucose flavonoid 3-O-glucosyltransferase 7 {ECO:0000303|PubMed:18487633};
DE            EC=2.4.1.91 {ECO:0000269|PubMed:18487633};
DE   AltName: Full=Flavonol 3-O-glucosyltransferase 7 {ECO:0000303|PubMed:18487633};
DE            Short=FaGT7 {ECO:0000303|PubMed:18487633};
GN   Name=GT7 {ECO:0000312|EMBL:ABB92749.1};
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:ABB92749.1}
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- and 4'-O-glucosides during fruit
CC       ripening. Accepted substrates include several flavonoids,
CC       hydroxycoumarins and beta-naphthols. Uses UDP-Glc as a sugar donor, but
CC       not UDP-Gal or UDP-GlcUA. May also be involved in detoxification of
CC       xenobiotics. {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=3.5 uM for isorhamnetin {ECO:0000269|PubMed:18487633};
CC         KM=0.6 mM for UDP-glucose {ECO:0000269|PubMed:18487633};
CC         Vmax=2.8 nmol/sec/mg enzyme with isorhamnetin as substrate
CC         {ECO:0000269|PubMed:18487633};
CC         Vmax=2.7 nmol/sec/mg enzyme with UDP-glucose as substrate
CC         {ECO:0000269|PubMed:18487633};
CC         Note=The kinetic constants are determined for the recombinant
CC         GST-fusion protein. {ECO:0000269|PubMed:18487633};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:18487633};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:18487633};
CC   -!- TISSUE SPECIFICITY: Strongly expressed in achenes and 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}.
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DR   EMBL; DQ289588; ABB92749.1; -; mRNA.
DR   AlphaFoldDB; Q2V6J9; -.
DR   SMR; Q2V6J9; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48047; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48047:SF45; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..487
FT                   /note="UDP-glucose flavonoid 3-O-glucosyltransferase 7"
FT                   /id="PRO_0000413770"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   ACT_SITE        121
FT                   /note="Charge relay"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         23
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         345
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         347
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         362
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         365
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         366
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         367
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         370
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         385
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         386
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         387
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
SQ   SEQUENCE   487 AA;  54652 MW;  313E7EB3889985FD CRC64;
     MAMETKSCQQ LHIFFLPFMA RGHSIPLTDI AKLFSSHGAR CTIVTTPLNA PLFSKATQRG
     EIELVLIKFP SAEAGLPQDC ESADLITTQD MLGKFVKATF LIEPHFEKIL DEHRPHCLVA
     DAFFTWATDV AAKFRIPRLY FHGTGFFALC ASLSVMMYQP HSNLSSDSES FVIPNLPDEI
     KMTRSQLPVF PDESEFMKML KASIEIEERS YGVIVNSFYE LEPAYANHYR KVFGRKAWHI
     GPVSFCNKAI EDKAERGSIK SSTAEKHECL KWLDSKKPRS VVYVSFGSMV RFADSQLLEI
     ATGLEASGQD FIWVVKKEKK EVEEWLPEGF EKRMEGKGLI IRDWAPQVLI LEHEAIGAFV
     THCGWNSILE AVSAGVPMIT WPVFGEQFYN EKLVTEIHRI GVPVGSEKWA LSFVDVNAET
     EGRVRREAIE EAVTRIMVGD EAVETRSRVK ELGENARRAV EEGGSSFLDL SALVGELNDL
     AFGGLVE
//