U71K2_PYRCO
ID U71K2_PYRCO Reviewed; 481 AA.
AC D3UAG2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=UDP-glycosyltransferase 71K2 {ECO:0000303|Ref.1};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=UDP-glucose:chalcone 2'-O-glucosyltransferase {ECO:0000305};
DE AltName: Full=UDP-glucose:flavonol 2'-O-glucosyltransferase {ECO:0000305};
GN Name=UGT71K2 {ECO:0000303|Ref.1};
OS Pyrus communis (Pear) (Pyrus domestica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=23211;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Abbe Fetel;
RX DOI=10.1016/j.plantsci.2009.12.009;
RA Gosch C., Halbwirth H., Schneider B., Holscher D., Stich K.;
RT "Cloning and heterologous expression of glycosyltransferases from Malus x
RT domestica and Pyrus communis, which convert phloretin to phloretin 2'-O-
RT glucoside (phloridzin).";
RL Plant Sci. 178:299-306(2010).
CC -!- FUNCTION: Glycosyltransferase that possesses chalcone and flavonol 2'-
CC O-glycosyltransferase activity. Converts phloretin to phlorizin
CC (phloretin 2'-O-glucoside), a potent antioxidant. Possesses
CC glycosyltransferase activity toward quercetin, isoliquiritigenin,
CC butein and caffeic acid. {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.25. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; FJ854495; ACZ44837.1; -; mRNA.
DR AlphaFoldDB; D3UAG2; -.
DR SMR; D3UAG2; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
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..481
FT /note="UDP-glycosyltransferase 71K2"
FT /id="PRO_0000434460"
FT BINDING 285
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 350..351
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 368..376
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 390..393
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ SEQUENCE 481 AA; 53299 MW; B8030DE6847B8904 CRC64;
MKKVELVFIP SPGAGHLVPT LQFAKRLIDR NDRISITILA IQSYFPTTLS SYTKSIAASE
PRIRFIDVPQ PQDRPPQEMY KSPAKFFSLY IESQVPSVKK IITNLVSSSA NSSDSIRVAA
LVVDLFCVSM IDVAKELNIP SYLFLTSNAG YLAFMLHLPI VNEKNQIAVE ESDPEWSIPG
IVHPVPPRVF PVALTDGRCS AYIKLASRFR ETRGIIVNTF VELETHAITL FSTDDGIPPV
YPVGPVIDMD DGQAHSNLDQ AQRDRIIKWL DDQPQKSVVF LCFGSMGSFR AEQVKEIALG
LEQSGQRFLW SLRMPSPIGT VPCDCSNLEE VLPDGFLERT NGKKGLICGW APQVEILAHS
ATGGFLSHCG WNSILESLWH GVPITTWPMY AEQQLNAFRM ARELGMALEM RLDYKRGSAD
VVGADEIERA VVGVMEKDSE VRKKVEEMGK MARKAVKDGG SSFASVGRFI EDVIGENSGF
K
