75L17_MALDO
ID 75L17_MALDO Reviewed; 481 AA.
AC A7MAS5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Phloretin 4'-O-glucosyltransferase {ECO:0000303|PubMed:27316677};
DE Short=MdPh-4'-OGT {ECO:0000303|PubMed:27316677};
DE EC=2.4.1.- {ECO:0000269|PubMed:27316677};
DE AltName: Full=Flavanone 7-O-beta-glucosyltransferase UGT75L17 {ECO:0000305};
DE EC=2.4.1.185 {ECO:0000269|PubMed:27316677};
DE AltName: Full=UDP-glycosyltransferase 75L17 {ECO:0000303|PubMed:27316677};
GN Name=UGT75L17 {ECO:0000303|PubMed:27316677};
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].
RX AGRICOLA=IND43942472;
RA Fischer T.C., Gosch C., Pfeiffer J., Halbwirth H., Halle C., Stich K.,
RA Forkmann G.;
RT "Flavonoid genes of pear (Pyrus communis).";
RL Trees 21:521-529(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=27316677; DOI=10.1016/j.phytochem.2016.06.004;
RA Yahyaa M., Davidovich-Rikanati R., Eyal Y., Sheachter A., Marzouk S.,
RA Lewinsohn E., Ibdah M.;
RT "Identification and characterization of UDP-glucose:Phloretin 4'-O-
RT glycosyltransferase from Malus x domestica Borkh.";
RL Phytochemistry 130:47-55(2016).
CC -!- FUNCTION: Glycosyltransferase that possesses phloretin 4'-O-
CC glycosyltransferase activity (PubMed:27316677). Converts phloretin to
CC trilobatin (phloretin 4'-O-glucoside), a potential antioxidant
CC (PubMed:27316677). Can convert with low efficiency phlorizin and
CC trilobatin to their corresponding di-O-glucosides (PubMed:27316677).
CC Can convert with low efficiency naringenin to naringenin-7-O-glucoside
CC (PubMed:27316677). Can convert with low efficiency quercetin to
CC quercetin-7-O-glucoside (PubMed:27316677).
CC {ECO:0000269|PubMed:27316677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phloretin + UDP-alpha-D-glucose = H(+) + trilobatin + UDP;
CC Xref=Rhea:RHEA:65148, ChEBI:CHEBI:15378, ChEBI:CHEBI:17276,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:145829;
CC Evidence={ECO:0000269|PubMed:27316677};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65149;
CC Evidence={ECO:0000269|PubMed:27316677};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-naringenin + UDP-alpha-D-glucose = (2S)-naringenin 7-O-
CC beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:65152,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17846, ChEBI:CHEBI:28327,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.185;
CC Evidence={ECO:0000269|PubMed:27316677};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65153;
CC Evidence={ECO:0000269|PubMed:27316677};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26.11 uM for phloretin {ECO:0000269|PubMed:27316677};
CC KM=1.19 mM for UDP-alpha-D-glucose {ECO:0000269|PubMed:27316677};
CC Vmax=1.86 pmol/sec/ug enzyme with phloretin as substrate
CC {ECO:0000269|PubMed:27316677};
CC Vmax=1.77 pmol/sec/ug enzyme with phloretin as substrate
CC {ECO:0000269|PubMed:27316677};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:27316677};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:27316677};
CC -!- TISSUE SPECIFICITY: Highly expressed in young leaves, at intermediate
CC level in mature leaves and at low levels in flowers and fruits.
CC {ECO:0000269|PubMed:27316677}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY786997; AAX16493.1; -; mRNA.
DR RefSeq; NP_001315912.1; NM_001328983.1.
DR AlphaFoldDB; A7MAS5; -.
DR SMR; A7MAS5; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GeneID; 103443397; -.
DR KEGG; mdm:103443397; -.
DR OrthoDB; 508327at2759; -.
DR GO; GO:0047243; F:flavanone 7-O-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008194; F:UDP-glycosyltransferase 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..481
FT /note="Phloretin 4'-O-glucosyltransferase"
FT /id="PRO_0000451483"
FT BINDING 289
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 351..352
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 369..377
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 391..394
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ SEQUENCE 481 AA; 53489 MW; C8C466A7B0EAC874 CRC64;
MVQHRFLLVT FPAQGHINPS LQFAKRLINT TGAHVTYVTS LSAHRRIGNG SIPDGLTYAP
FSDGYDDGFK PGDNVDDYMS ELRRRGVQAI TDLVVASANE GHPYTCLVYS LLLPWSAGMA
HELHLPSVLL WIQPATVFDI YYYYFNGYKD LIRDNTSSGT NNVLPCSIEL PGLPLSFTSR
DLPSFMVDTN PYNFALPLFQ EQMELLERET NPTILVNTFD ALEPEALKAI DKYNLIGVGP
LIPSAFLDGK DPSDKSFGGD LFQKSKDSSY LEWLNSKPEG SVIYVSFGSI SVLGKAQMEE
IAKGLLDCGL PFLWVIRDKV GKKGDDNEAK KEEEMLRCRE ELEELGMIVP WCSQVEVLSS
PSLGCFVTHC GWNSSLESLV SGVPVVAFPQ WTDQGTNAKL IEDYWKTGVR VTPNEEGIVT
GEELKRCLDL VLGSGEIGED VRRNAKKWKD LAREAVSEGD SSDKNLRAFL DQIKVLKDAR
H
