ID   U88F2_PYRCO             Reviewed;         483 AA.
AC   D3UAG3;
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=Phloretin 2'-O-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000269|Ref.1};
DE   AltName: Full=UDP-glucose:phloretin 2'-O-glucosyltransferase {ECO:0000305};
DE   AltName: Full=UDP-glycosyltransferase 88F2 {ECO:0000303|Ref.1};
GN   Name=UGT88F2 {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, CATALYTIC ACTIVITY, AND
RP   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 phloretin 2'-O-
CC       glycosyltransferase activity. Converts phloretin to phlorizin
CC       (phloretin 2'-O-glucoside), a potent antioxidant. Is specific for
CC       phloretin and does not possess glycosyltransferase activity toward
CC       naringenin, naringenin chalcone, eriodictyol, eriodictyol chalcone,
CC       apigenin, luteolin, kaempferol, quercetin, isoliquiritigenin, butein,
CC       caffeic acid, 2-coumaric acid, 3-coumaric acid, 3-hydroxybenzoic acid,
CC       3,4-dihydroxybenzoic acid and 3,4-dihydroxyhydrocinnamic acid (Ref.1).
CC       Can glycosylate phloretin in the presence of UDP-glucose, UDP-xylose
CC       and UDP-galactose (By similarity). {ECO:0000250|UniProtKB:B3TKC8,
CC       ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phloretin + UDP-alpha-D-glucose = H(+) + phlorizin + UDP;
CC         Xref=Rhea:RHEA:51576, ChEBI:CHEBI:8113, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17276, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         Evidence={ECO:0000269|Ref.1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ854496; ACZ44838.1; -; mRNA.
DR   AlphaFoldDB; D3UAG3; -.
DR   SMR; D3UAG3; -.
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..483
FT                   /note="Phloretin 2'-O-glucosyltransferase"
FT                   /id="PRO_0000434453"
FT   BINDING         290
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         359..360
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         377..385
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         399..402
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   483 AA;  53522 MW;  2E5DCA59708CA9A2 CRC64;
     MGDVIVLYAS PGMGHIVAMV ELGKFIVHRY GPHKFSITIL YTCGSIVDTA SIPVYIRRIS
     HSHPFISFRQ FPRVTNNITR NISVPAITFD FIRQNDPHVR SALQEISKSA TVRAFIIDLF
     CTSALPIGKE FNIPTYYFHT SGAAVLAAFL YLPKIDEQTK TTESFKDLRD TVFEFPGWKS
     PLKATHMVQL VLDRNDPAYS DMIYFCSHLP KSNGIIVNTF EELEPPSVLQ AIAGGLCVPD
     GPTPPVYYVG PLIEEEKELS KDADAAEKED CLSWLDKQPS RSVLFLCFGS MGSFPAAQLK
     EIANGLEASG QRFLWVVKKP PVEEKSKQVH GVDDFDLKGV LPEGFLERTA DRGMVVKSWA
     PQVVVLKKES VGGFVTHCGW NSVLEAVVAG VPMIAWPLYA EQHMNRNVLV TDMEIAIGVE
     QRDEEGGFVS GEEVERRVRE LMESEGGRAL RERCKKLGEM ASAALGETGS STRNLVNFVS
     SIT