U71K1_MALDO
ID U71K1_MALDO Reviewed; 477 AA.
AC D3UAG0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=UDP-glycosyltransferase 71K1 {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=UGT71K1 {ECO:0000303|Ref.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Rebella;
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 6.75. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; FJ854493; ACZ44835.1; -; mRNA.
DR RefSeq; NP_001280899.1; NM_001293970.1.
DR AlphaFoldDB; D3UAG0; -.
DR SMR; D3UAG0; -.
DR STRING; 3750.XP_008384821.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GeneID; 103447413; -.
DR KEGG; mdm:103447413; -.
DR OrthoDB; 508327at2759; -.
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..477
FT /note="UDP-glycosyltransferase 71K1"
FT /id="PRO_0000434459"
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 477 AA; 52843 MW; 3B7F9C107B68747F CRC64;
MKKVELVFIP SPGAGHHLPT LQFVKRLIDR NDRISITILA IQSYFPTTLS SYTKSIAASE
PRIRFIDVPQ PQDRPPQEMY KSRAQIFSLY IESHVPSVKK IITNLVSSSA NSSDSIRVAA
LVVDLFCVSM IDVAKELNIP SYLFLTSNAG YLAFMLHLPI LHEKNQIAVE ESDPDWSIPG
IVHPVPPRVL PAALTDGRLS AYIKLASRFR ETRGIIVNTF VELETHAITL FSNDDRVPPV
YPVGPVIDLD DGQEHSNLDQ AQRDKIIKWL DDQPQKSVVF LCFGSMGSFG AEQVKEIAVG
LEQSGQRFLW SLRMPSPKGI VPSDCSNLEE VLPDGFLERT NGKKGLICGW APQVEILAHS
ATGGFLSHCG WNSILESLWH GVPIATWPMY AEQQLNAFRM VRELGMALEM RLDYKAGSAD
VVGADEIEKA VVGVMEKDSE VRKKVEEMGK MARKAVKDGG SSFASVGRFI EDVIGQN