ID   U7A15_MALDO             Reviewed;         471 AA.
AC   D3THI6;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=UDP-glycosyltransferase 71A15 {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=UGT71A15 {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, naringenin, naringenin chalcone,
CC       eriodictyol, eriodictyol chalcone, apigenin, luteolin, kaempferol,
CC       quercetin, isoliquiritigenin, butein and caffeic acid. Can convert
CC       phloretin to phloretin 4'-O-glucoside and phloretin 4-O-glucoside.
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; DQ103712; AAZ80472.1; -; mRNA.
DR   RefSeq; NP_001315903.1; NM_001328974.1.
DR   AlphaFoldDB; D3THI6; -.
DR   SMR; D3THI6; -.
DR   STRING; 3750.XP_008378326.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 103441425; -.
DR   KEGG; mdm:103441425; -.
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..471
FT                   /note="UDP-glycosyltransferase 71A15"
FT                   /id="PRO_0000434457"
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;  51997 MW;  1D74EA284C553CD0 CRC64;
     MKRPAQLVFV PAPGIGHIVS TVEMAKQLAA RDDQLFITVL VMKLPYAQPF TNTDSSISHR
     INFVNLPEAQ PDKQDIVPNP GSFFRMFVEN HKSHVRDAVI NVLPESDQSE STSKPRLAGF
     VLDMFSASLI DVANEFKVPS YLFFTSNASA LALMSHFQSL RDEGGIDITE LTSSTAELAV
     PSFINPYPAA VLPGSLLDME STKSTLNHVS KYKQTKGILV NTFMELESHA LHYLDSGDKI
     PPVYPVGPLL NLKSSDEDKA SDILRWLDDQ PPFSVVFLCF GSMGSFGEAQ VKEIACALEH
     SGHRFLWSLR RPPPQGKRAM PSDYEDLKTV LPEGFLDRTA TVGKVIGWAP QAAILGHPAT
     GGFVSHCGWN STLESLWNGV PIAAWPLYAE QNLNAFQLVV ELGLAVEIKM DYRRDSDVVV
     SAEDIERGIR RVMELDSDVR KRVKEMSEKS KKALVDGGSS YSSLGRFIDK I