UFOG2_FRAAN
ID UFOG2_FRAAN Reviewed; 465 AA.
AC Q5UL10; Q5UL11; Q6PVW5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Anthocyanidin 3-O-glucosyltransferase 2;
DE EC=2.4.1.115 {ECO:0000269|PubMed:17573033};
DE AltName: Full=UDP-glucose flavonoid 3-O-glucosyltransferase 2 {ECO:0000312|EMBL:AAS89832.1};
DE Short=FaFGT {ECO:0000303|PubMed:17573033};
GN Name=FGT {ECO:0000312|EMBL:AAU12367.1};
GN Synonyms=UFGT {ECO:0000312|EMBL:AAS89832.1};
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:AAU12367.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Queen Elisa {ECO:0000269|PubMed:17573033};
RC TISSUE=Fruit {ECO:0000269|PubMed:17573033}, and
RC Leaf {ECO:0000269|PubMed:17573033};
RX PubMed=17573033; DOI=10.1016/j.abb.2007.04.040;
RA Almeida J.R., D'Amico E., Preuss A., Carbone F., de Vos C.H., Deiml B.,
RA Mourgues F., Perrotta G., Fischer T.C., Bovy A.G., Martens S., Rosati C.;
RT "Characterization of major enzymes and genes involved in flavonoid and
RT proanthocyanidin biosynthesis during fruit development in strawberry
RT (Fragaria x ananassa).";
RL Arch. Biochem. Biophys. 465:61-71(2007).
RN [2] {ECO:0000312|EMBL:AAS89832.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Munoz-Blanco J., Caballero J.L., Moyano E., Lopez-Raez J.A.;
RT "An UDP glucose:flavonoid-3-O-glucosyltransferase gene along strawberry
RT fruit ripening.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In the presence of other necessary color factors, this
CC glycosylation reaction allows the accumulation of anthocyanin pigments
CC (PubMed:17573033). Anthocyanidins are the preferred substrates, while
CC flavonols are only a minor substrate in vitro (PubMed:17573033).
CC {ECO:0000269|PubMed:17573033}.
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:17573033};
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:17573033};
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:17573033};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC {ECO:0000269|PubMed:17573033}.
CC -!- TISSUE SPECIFICITY: Highest expression detected in fruit, with very low
CC levels detected in petal and leaf. {ECO:0000269|PubMed:17573033}.
CC -!- DEVELOPMENTAL STAGE: Expression in fruit is ripening-related, with
CC highest expression levels detected in turning stage and red fruit.
CC {ECO:0000269|PubMed:17573033}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000255}.
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DR EMBL; AY695815; AAU12366.1; -; mRNA.
DR EMBL; AY695816; AAU12367.1; -; Genomic_DNA.
DR EMBL; AY575056; AAS89832.1; -; mRNA.
DR AlphaFoldDB; Q5UL10; -.
DR SMR; Q5UL10; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PRIDE; Q5UL10; -.
DR UniPathway; UPA00009; -.
DR GO; GO:0047213; F:anthocyanidin 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..465
FT /note="Anthocyanidin 3-O-glucosyltransferase 2"
FT /id="PRO_0000413767"
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 318
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
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:P51094"
FT BINDING 386..387
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P51094"
FT CONFLICT 1..4
FT /note="MAPV -> MA (in Ref. 1; AAU12366 and 2; AAS89832)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> S (in Ref. 2; AAS89832)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..358
FT /note="QVLAHGSVGA -> TGPGAWFSWS (in Ref. 2; AAS89832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 50353 MW; E6C8BFAFDB6FF64B CRC64;
MAPVSNQAGG HVAVLAFPFS THAAPLLNIV CRLAAAAPST LFSFFNTKQS NSSILASDTS
VLRYTNVCVC EVADGVPEGY VFVGKPQEDI ELFMKAAPDN FRKCLEASVA ESGREVSCLV
TDAFFWFGAH MADDMGGVPW VPFWTAGPAS LSAHVHTDLI RNTTSGDCHD EKETITVIAG
MSKVRPQDLP EGIIFGNLES LFSRMLHQMG LMLPLATAVF INSFEELDPV ITNDLKSKFK
RFLNVGPLDL LEPTASAATT TPQTAEAVAG DGCLSWLDKQ KAASVVYVSF GSVTRPSPEE
LMALAEALEA SRVPFLWSLR DNLKNPQLDE FLSKGKLNGM VVPWAPQPQV LAHGSVGAFV
THCGWNSVLE SVAGGVPLIC RPFFGDQKLN ARMVEDVWKI GLRLEGGVFT KNGMLKSLDM
LLSQDKGTKM KNKIHTLKQL AQQAVEPKGS STRNFESLLE MATTN
