U7A16_PYRCO
ID U7A16_PYRCO Reviewed; 471 AA.
AC D3UAG1;
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 71A16 {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=UGT71A16 {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 eriodictyol, apigenin, luteolin,
CC kaempferol, quercetin, isoliquiritigenin, butein and caffeic acid.
CC {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 30 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; FJ854494; ACZ44836.1; -; mRNA.
DR AlphaFoldDB; D3UAG1; -.
DR SMR; D3UAG1; -.
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..471
FT /note="UDP-glycosyltransferase 71A16"
FT /id="PRO_0000434458"
FT BINDING 282
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 348..349
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 366..374
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 388..391
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ SEQUENCE 471 AA; 52002 MW; 64AC8506B1D011F6 CRC64;
MKRSAQLVFV PAPGIGHIVS TVEMAKQLVA RDDQLFITVL VMKLPYDQPF TNTDSSISHR
INFVNLPEAQ LDKQDTVPNP GSFFRMFVEN HKTHVRDAVI NLLPESDQSE STSKPRLAGF
VLDMFSASLI DVANEFEVPS YVFFTSNSST LALLSHFQSL RDEGGIDITE LTSSTAELAV
PSFINPYPVA VLPGSFLDKE STKSTLNNVG RYKQTKGILV NTFLELESHA LHYLDSGVKI
PPVYPVGPLL NLKSSHEDKG SDILRWLDDQ PPLSVVFLCF GSMGSFGDAQ VKEIACTLEH
SGHRFLWSLR QPPSKGKRAL PSDYADLKTV LPEGFLDRTA TVGRVIGWAP QAAILGHPAI
GGFVSHCGWN STLESIWNGV PIAAWPMYAE QNMNAFQLVV ELGLAVEIKM DYRKDSDVVV
SAEDIERGIR QVMELDSDVR KRVKEMSEKS KKALVDGGSS YSSLGRFIDQ I
