ID   U88F5_MALDO             Reviewed;         481 AA.
AC   D3UAG6;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=UDP-glycosyltransferase 88F5 {ECO:0000303|Ref.1};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=UDP-glucose:chalcone 2'-O-glucosyltransferase {ECO:0000305};
GN   Name=UGT88F5 {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; FJ854499; ACZ44841.1; -; mRNA.
DR   RefSeq; NP_001315799.1; NM_001328870.1.
DR   AlphaFoldDB; D3UAG6; -.
DR   SMR; D3UAG6; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 103425310; -.
DR   KEGG; mdm:103425310; -.
DR   OrthoDB; 508327at2759; -.
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 88F5"
FT                   /id="PRO_0000434456"
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;  53205 MW;  5E4B6AA474F34F75 CRC64;
     MGDVIVLYAA PGIGHIVSMV ELGKLIVHRY GPHKFSITIL YTCGSVVDIT SIPAYIRRIS
     HSHPSISFLQ FPRVTNKITR NISGAAIMFD FIRQNDPHVR RALQEISKSA AVRAFIIDLF
     CTSALPIGKE FNIPTYYFYT SGAAALAAFL YFPKIDEQTT ESFKDLRETV FEFPGWKSPL
     KAIHMVEPVL DRNDPAYSDM IYFCSQLPKS NGIIVNTFEE LEPPSVLQAI AGGLCVPDGP
     TPPVYYVGPL IEEEKELSKD ADAAEKEDCL SWLDKQPSRS VLFLCFGSMG SFPAAQLKEI
     ANGLEASGQR FLWVVKKPPV EEKSKQVHGV DDFDLKGVLP EGFLERTADR GMVVKSWAPQ
     VVVLKKESVG GFVTHCGWNS VLEAVVAGVP MIAWPLYAEQ HMNRNVLVTD MEIAIGVEQR
     DEEGGFVSGE EVERRVRELM ESEGGRALRE RCKKLGEMAS AALGETGSST RNMVNFVSSI
     T