UFOG1_FRAAN
ID UFOG1_FRAAN Reviewed; 466 AA.
AC Q66PF5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Anthocyanidin 3-O-glucosyltransferase 1;
DE Short=FaGT1 {ECO:0000303|PubMed:18258692};
DE EC=2.4.1.115 {ECO:0000269|PubMed:18258692};
DE AltName: Full=Flavonol 3-O-glucosyltransferase {ECO:0000305};
DE EC=2.4.1.91 {ECO:0000269|PubMed:18258692};
GN Name=GT1 {ECO:0000303|PubMed:18258692};
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Elsanta {ECO:0000312|EMBL:AAU09442.1};
RX PubMed=16443693; DOI=10.1104/pp.105.074955;
RA Lunkenbein S., Bellido M., Aharoni A., Salentijn E.M., Kaldenhoff R.,
RA Coiner H.A., Munoz-Blanco J., Schwab W.;
RT "Cinnamate metabolism in ripening fruit. Characterization of a UDP-
RT glucose:cinnamate glucosyltransferase from strawberry.";
RL Plant Physiol. 140:1047-1058(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=cv. Elsanta {ECO:0000269|PubMed:18258692};
RC TISSUE=Leaf {ECO:0000269|PubMed:18258692};
RX PubMed=18258692; DOI=10.1104/pp.107.114280;
RA Griesser M., Hoffmann T., Bellido M.L., Rosati C., Fink B., Kurtzer R.,
RA Aharoni A., Munoz-Blanco J., Schwab W.;
RT "Redirection of flavonoid biosynthesis through the down-regulation of an
RT anthocyanidin glucosyltransferase in ripening strawberry fruit.";
RL Plant Physiol. 146:1528-1539(2008).
CC -!- FUNCTION: In the presence of other necessary color factors, this
CC glycosylation reaction allows the accumulation of anthocyanin pigments
CC (Probable). Uses UDP-Glc as a sugar donor, but not UDP-Gal or UDP-GlcUA
CC (PubMed:18258692). Anthocyanidins are the preferred substrates in vivo,
CC but flavonols can also be glucosylated in vitro (PubMed:18258692).
CC {ECO:0000269|PubMed:18258692, ECO:0000305|PubMed:18258692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an anthocyanidin + H(+) + UDP-alpha-D-glucose = an
CC anthocyanidin 3-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:20093,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16307, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:143576; EC=2.4.1.115;
CC Evidence={ECO:0000269|PubMed:18258692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20094;
CC Evidence={ECO:0000269|PubMed:18258692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyanidin + UDP-alpha-D-glucose = cyanidin 3-O-beta-D-glucoside
CC + H(+) + UDP; Xref=Rhea:RHEA:60100, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:71682,
CC ChEBI:CHEBI:77857; EC=2.4.1.115;
CC Evidence={ECO:0000269|PubMed:18258692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60101;
CC Evidence={ECO:0000269|PubMed:18258692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pelargonidin + UDP-alpha-D-glucose = pelargonidin 3-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61504, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:144777, ChEBI:CHEBI:144778;
CC EC=2.4.1.115; Evidence={ECO:0000269|PubMed:18258692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61505;
CC Evidence={ECO:0000269|PubMed:18258692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peonidin + UDP-alpha-D-glucose = peonidin 3-O-beta-D-glucoside
CC + UDP; Xref=Rhea:RHEA:61508, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:144779, ChEBI:CHEBI:144780; EC=2.4.1.115;
CC Evidence={ECO:0000269|PubMed:18258692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61509;
CC Evidence={ECO:0000269|PubMed:18258692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=delphinidin + UDP-alpha-D-glucose = delphinidin 3-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61500, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:144775, ChEBI:CHEBI:144776;
CC EC=2.4.1.115; Evidence={ECO:0000269|PubMed:18258692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61501;
CC Evidence={ECO:0000269|PubMed:18258692};
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:18258692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22301;
CC Evidence={ECO:0000269|PubMed:18258692};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for pelargonidin {ECO:0000269|PubMed:18258692};
CC KM=1.1 mM for UDP-glucose {ECO:0000269|PubMed:18258692};
CC Vmax=21 nmol/sec/mg enzyme with pelargonidin as substrate
CC {ECO:0000269|PubMed:18258692};
CC Vmax=73 nmol/sec/mg enzyme with UDP-glucose as substrate
CC {ECO:0000269|PubMed:18258692};
CC Note=The kinetic constants are determined for the recombinant His(6)-
CC tagged protein. {ECO:0000269|PubMed:18258692};
CC pH dependence:
CC Optimum pH is 7-8 with pelargonidin and cyanidin as substrates.
CC {ECO:0000269|PubMed:18258692};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius with pelargonidin and
CC cyanidin as substrates. {ECO:0000269|PubMed:18258692};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC {ECO:0000269|PubMed:18258692}.
CC -!- TISSUE SPECIFICITY: Highest expression detected in receptacles and
CC achenes, with very low levels detected in runners, leaves, flowers,
CC crowns and green receptacles. {ECO:0000269|PubMed:18258692}.
CC -!- DEVELOPMENTAL STAGE: Expression in achenes and receptacles is ripening-
CC related, with highest expression levels detected in fully ripe red
CC receptacles. {ECO:0000269|PubMed:18258692}.
CC -!- INDUCTION: By de-achening. Down-regulated by synthetic auxin
CC naphthaleneacetic acid (NAA). {ECO:0000269|PubMed:18258692}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000255}.
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DR EMBL; AY663784; AAU09442.1; -; mRNA.
DR AlphaFoldDB; Q66PF5; -.
DR SMR; Q66PF5; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR UniPathway; UPA00009; -.
DR GO; GO:0047213; F:anthocyanidin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
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 GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
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..466
FT /note="Anthocyanidin 3-O-glucosyltransferase 1"
FT /id="PRO_0000413766"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 21
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 145
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 319
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 346
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT BINDING 387..388
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P51094"
SQ SEQUENCE 466 AA; 50456 MW; E19385E45790BDA5 CRC64;
MAPVSNQVGG HVAVLAFPFS THAAPLLNIV CRLAAAAPST LFSFFNTKQS NSSILAGNTS
VLRYSNVSVC EVADGVPEGY VFVGKPQEDI ELFMKAAPDN FRRCLEASVA ESGREVSCLV
TDAFFWFGVH MADDMGGVPW VPFWTAGPAS LSAHVHTDLI RSTTSGGCHD EKETITVIAG
MSKVRPQDLP EGIIFGNLES LFSRMLHQMG QMPPLATAVF INSFEELDPV ITNDLKSKFK
RFLNVGPLDL LEPPASAATT TPQTAAEAVA GDGCLSWLDE QKVASVVYVS FGSVTRPSPE
ELMALAEALE ASRVPFLWSL RDNLKNRQLD EFLSKGKLNG MVVPWAPQPQ VLAHGSVGAF
VTHCGWNSVL ESVAGGVPLI CRPFFGDQKL NARMVEDVWK IGLRLEGGVF TKNGMLKSLD
MLLSQDKGTK MKNKINTLKQ FAKQAVEPKG SSARNFESLL EMTTTN
