ID   U88F3_PYRCO             Reviewed;         481 AA.
AC   D3UAG7;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=UDP-glycosyltransferase 88F3 {ECO:0000303|Ref.1};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=UDP-glucose:chalcone 2'-O-glucosyltransferase {ECO:0000305};
GN   Name=UGT88F3 {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].
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 may possess chalcone and
CC       dihydrochalcone 2'-O-glucosyltransferase activity.
CC       {ECO:0000250|UniProtKB:D3UAG3}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ854500; ACZ44842.1; -; mRNA.
DR   AlphaFoldDB; D3UAG7; -.
DR   SMR; D3UAG7; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..481
FT                   /note="UDP-glycosyltransferase 88F3"
FT                   /id="PRO_0000434454"
FT   BINDING         288
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         357..358
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         375..383
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         397..400
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   481 AA;  53381 MW;  B27D4C213B429155 CRC64;
     MGDVIVLYAA PGMGHIVSMV ELGKLIVHRY GPHKFSITIL YTCGSVVDTT SIPAYIRRIS
     HSHPSISFCQ FPRVTNKITP NISGAAIMFD FIRQNDPHVR RALQEISKSA AVRAFVIDLF
     CTSALPIGKE FNIPTYYFHT SGAAVLAAFL YFPKIDEQTT DSFKDLRDTV FEFPGWKSPL
     KAIHMVEPVL DRNDPAYSDM IYFCSHLPKS NGIVVNTFEE LEPPTILQAI AGGLCVPDGP
     TPPVYYVGPL IDEEKELSND AAAAEEEDCL SWLDKQPRRS VLFLCFGSRG SFPAVQLKEI
     ANGLEASGQR FLWVVKKPPV EEKTKQVHGV DDFDLEAVLP EGFLERTADR GMVVKSWAPQ
     VVVLKKESVG GFVTHCGWNS VLEAVVAGVP MIAWPLYAEQ QMNRNVLVTD MEMAIGVEQR
     DEEDGFVNAE EVERRVRELM ESEGGRLLRE RCKKMGEMAL AALGETGSST RNLVNFVSSI
     T