ID   U88F4_MALDO             Reviewed;         481 AA.
AC   D3UAG4;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=UDP-glycosyltransferase 88F4 {ECO:0000303|Ref.1};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=UDP-glucose:chalcone 2'-O-glucosyltransferase {ECO:0000305};
GN   Name=UGT88F4 {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].
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 may possess chalcone and
CC       dihydrochalcone 2'-O-glucosyltransferase activity.
CC       {ECO:0000250|UniProtKB:B3TKC8}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ854497; ACZ44839.1; -; mRNA.
DR   AlphaFoldDB; D3UAG4; -.
DR   SMR; D3UAG4; -.
DR   STRING; 3750.XP_008361616.1; -.
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 88F4"
FT                   /id="PRO_0000434455"
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;  53401 MW;  863FCBC1765E4297 CRC64;
     MGDVIVLYAA PGMGHIVSMV ELGKLIVHRY GPHKFSITIL YTCGSVVDIT SISAYIRRIS
     HSHPSISFRQ FPRVTNKITR NISGAAIMFD FIRQNDPHVR RALQEISKSV AVRAFIIDLF
     CTSALPIGKE FNIPTYYFYT SGAAALAAFL YFPKIDEQTT ESFQDLRDTV FEFPGWKSPL
     KAIHMVEPVL DRNDPAYSDM IYFCSQLPKS NGIIVNTFEE LESSNVLQAI AGGLCVPDGP
     TPPVYYVGPL IDEEKELSND AAAAEEEDCL SWLDKQPSRS VLFLCFGSRG SFPAVQLKEI
     ANGLEASGQR FLWVVKKPPV EEKTKQVHGV DDFDLKGVLP EGFLERTADR GMVVKSWAPQ
     VVVLKKESVG GFVTHCGWNS VLEAVVAGVP MIAWPLYAEQ HMNRNVLVTD MEIAIGVEQR
     DEEDGFVSGE EVERRVRELM ESEGGRVLRE RCKKIGEMAL AALGETGSST RNFVNFVSSI
     T