ID   88F1R_MALDO             Reviewed;         483 AA.
AC   D3UAG5;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Phloretin 2'-O-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.357 {ECO:0000250|UniProtKB:B3TKC8};
DE   AltName: Full=UDP-glucose:phloretin 2'-O-glucosyltransferase {ECO:0000305};
DE   AltName: Full=UDP-glycosyltransferase 88F1 {ECO:0000303|Ref.1};
GN   Name=UGT88F1 {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 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       caffeic acid, catechin, chlorogenic acid, 2-coumaric acid, 3-coumaric
CC       acid, 4-coumaric acid, cyanidin, 3,4-dihydroxyhydrocinnamic acid,
CC       epicatechin, 3-hydroxybenzoic acid, naringenin, 3,4-dihydroxybenzoic
CC       acid, quercetin and rutin. Can glycosylate phloretin in the presence of
CC       UDP-glucose, UDP-xylose and UDP-galactose.
CC       {ECO:0000250|UniProtKB:B3TKC8}.
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         EC=2.4.1.357; Evidence={ECO:0000250|UniProtKB:B3TKC8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51577;
CC         Evidence={ECO:0000250|UniProtKB:B3TKC8};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ854498; ACZ44840.1; -; mRNA.
DR   AlphaFoldDB; D3UAG5; -.
DR   SMR; D3UAG5; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   BRENDA; 2.4.1.357; 3164.
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..483
FT                   /note="Phloretin 2'-O-glucosyltransferase"
FT                   /id="PRO_0000434452"
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;  53600 MW;  34F566676E7556F6 CRC64;
     MGDVIVLYAS PGMGHIVSMV ELGKFIVHRY GPHKFSITIL YTCGSIVDTA SIPVYIRRIS
     HSHPFISFRQ FPRVTNNITR NISVPAITFD FIRQNDPHVR SALQEISKSA TVRAFIIDLF
     CTSALPIGKE FNIPTYYFRT SGAAILAAFL 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 LMESEGGRVL RERCKKLGEM ASAALGETGS STRNLVNFVS
     SIT