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Anthocyanidin 3-O-glucosyltransferase 2 (EC 2.4.1.115) (UDP-glucose flavonoid 3-O-glucosyltransferase 2) (FaFGT)

 UFOG2_FRAAN             Reviewed;         465 AA.
Q5UL10; Q5UL11; Q6PVW5;
16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
05-DEC-2018, entry version 42.
RecName: Full=Anthocyanidin 3-O-glucosyltransferase 2;
EC=2.4.1.115 {ECO:0000269|PubMed:17573033};
AltName: Full=UDP-glucose flavonoid 3-O-glucosyltransferase 2 {ECO:0000312|EMBL:AAS89832.1};
Short=FaFGT {ECO:0000303|PubMed:17573033};
Name=FGT {ECO:0000312|EMBL:AAU12367.1};
Synonyms=UFGT {ECO:0000312|EMBL:AAS89832.1};
Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria
virginiana).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Rosales; Rosaceae; Rosoideae;
Potentilleae; Fragariinae; Fragaria.
NCBI_TaxID=3747;
[1] {ECO:0000305, ECO:0000312|EMBL:AAU12367.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC
ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Queen Elisa {ECO:0000269|PubMed:17573033};
TISSUE=Fruit {ECO:0000269|PubMed:17573033}, and
Leaf {ECO:0000269|PubMed:17573033};
PubMed=17573033; DOI=10.1016/j.abb.2007.04.040;
Almeida J.R., D'Amico E., Preuss A., Carbone F., de Vos C.H.,
Deiml B., Mourgues F., Perrotta G., Fischer T.C., Bovy A.G.,
Martens S., Rosati C.;
"Characterization of major enzymes and genes involved in flavonoid and
proanthocyanidin biosynthesis during fruit development in strawberry
(Fragaria x ananassa).";
Arch. Biochem. Biophys. 465:61-71(2007).
[2] {ECO:0000312|EMBL:AAS89832.1}
NUCLEOTIDE SEQUENCE [MRNA].
Munoz-Blanco J., Caballero J.L., Moyano E., Lopez-Raez J.A.;
"An UDP glucose:flavonoid-3-O-glucosyltransferase gene along
strawberry fruit ripening.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: In the presence of other necessary color factors, this
glycosylation reaction allows the accumulation of anthocyanin
pigments. Anthocyanidins are the preferred substrates, while
flavonols are only a minor substrate in vitro.
{ECO:0000269|PubMed:17573033}.
-!- CATALYTIC ACTIVITY:
Reaction=UDP-D-glucose + an anthocyanidin = UDP + an
anthocyanidin-3-O-beta-D-glucoside.; EC=2.4.1.115;
Evidence={ECO:0000269|PubMed:17573033};
-!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
{ECO:0000269|PubMed:17573033}.
-!- TISSUE SPECIFICITY: Highest expression detected in fruit, with
very low levels detected in petal and leaf.
{ECO:0000269|PubMed:17573033}.
-!- DEVELOPMENTAL STAGE: Expression in fruit is ripening-related, with
highest expression levels detected in turning stage and red fruit.
{ECO:0000269|PubMed:17573033}.
-!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
{ECO:0000255}.
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EMBL; AY695815; AAU12366.1; -; mRNA.
EMBL; AY695816; AAU12367.1; -; Genomic_DNA.
EMBL; AY575056; AAS89832.1; -; mRNA.
ProteinModelPortal; Q5UL10; -.
SMR; Q5UL10; -.
CAZy; GT1; Glycosyltransferase Family 1.
UniPathway; UPA00009; -.
GO; GO:0047213; F:anthocyanidin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR002213; UDP_glucos_trans.
InterPro; IPR035595; UDP_glycos_trans_CS.
Pfam; PF00201; UDPGT; 1.
PROSITE; PS00375; UDPGT; 1.
1: Evidence at protein level;
Glycosyltransferase; Transferase.
CHAIN 1 465 Anthocyanidin 3-O-glucosyltransferase 2.
/FTId=PRO_0000413767.
REGION 386 387 UDP-D-glucose binding.
{ECO:0000250|UniProtKB:P51094}.
BINDING 20 20 Substrate.
{ECO:0000250|UniProtKB:P51094}.
BINDING 21 21 UDP-D-glucose.
{ECO:0000250|UniProtKB:P51094}.
BINDING 22 22 Substrate.
{ECO:0000250|UniProtKB:P51094}.
BINDING 87 87 Substrate.
{ECO:0000250|UniProtKB:P51094}.
BINDING 145 145 UDP-D-glucose.
{ECO:0000250|UniProtKB:P51094}.
BINDING 154 154 Substrate.
{ECO:0000250|UniProtKB:P51094}.
BINDING 318 318 UDP-D-glucose.
{ECO:0000250|UniProtKB:P51094}.
BINDING 345 345 UDP-D-glucose; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P51094}.
CONFLICT 1 4 MAPV -> MA (in Ref. 1; AAU12366 and 2;
AAS89832). {ECO:0000305}.
CONFLICT 123 123 A -> S (in Ref. 2; AAS89832).
{ECO:0000305}.
CONFLICT 349 358 QVLAHGSVGA -> TGPGAWFSWS (in Ref. 2;
AAS89832). {ECO:0000305}.
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


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