ID   88F1G_MALDO             Reviewed;         483 AA.
AC   B3TKC8; V5REG9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Phloretin 2'-O-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.357 {ECO:0000269|PubMed:18573104};
DE   AltName: Full=Phloretin glucosyltransferase 1 {ECO:0000303|PubMed:18573104};
DE            Short=MdPGT1 {ECO:0000303|PubMed:18573104};
DE   AltName: Full=UDP-glucose:phloretin 2'-O-glucosyltransferase {ECO:0000305};
DE   AltName: Full=UDP-glycosyltransferase 88F1 {ECO:0000303|PubMed:18573104};
GN   Name=UGT88F1 {ECO:0000303|PubMed:18573104};
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, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Royal Gala;
RX   PubMed=18573104; DOI=10.1111/j.1742-4658.2008.06526.x;
RA   Jugde H., Nguy D., Moller I., Cooney J.M., Atkinson R.G.;
RT   "Isolation and characterization of a novel glycosyltransferase that
RT   converts phloretin to phlorizin, a potent antioxidant in apple.";
RL   FEBS J. 275:3804-3814(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Golden Delicious;
RA   Xu Y.;
RT   "Cloning and bioinformatic analysis of phloridzin glycosyltransferase from
RT   Malus domestica.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:18573104}.
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:0000269|PubMed:18573104};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51577;
CC         Evidence={ECO:0000269|PubMed:18573104};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.62 uM for phloretin {ECO:0000269|PubMed:18573104};
CC         KM=13 uM for UDP-glucose {ECO:0000269|PubMed:18573104};
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:18573104};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:18573104};
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC       leaves, flowers and fruits. {ECO:0000269|PubMed:18573104}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; EU246349; ABY73540.1; -; mRNA.
DR   EMBL; KF574084; AHB33773.1; -; mRNA.
DR   AlphaFoldDB; B3TKC8; -.
DR   SMR; B3TKC8; -.
DR   STRING; 3750.XP_008339149.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   BioCyc; MetaCyc:MON-15672; -.
DR   BRENDA; 2.4.1.357; 3164.
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_0000434451"
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;  53547 MW;  C55F77C67034BDB8 CRC64;
     MGDVIVLYAS PGMGHIVSMV ELGKFIVHRY GPHKFSITIL YTCGSIVDTA SIPVYIRRIS
     HSHPFISFRQ FPRVTNNITR NISVPAITFD FIRQNDPHVR SALQEISKSA TVRAFIIDLF
     CTSALPIGKE FNIPTYYFCT 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