ID   GGT_QUERO               Reviewed;         510 AA.
AC   V5LLZ9;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Gallate 1-beta-glucosyltransferase {ECO:0000303|PubMed:24412325};
DE            EC=2.4.1.136 {ECO:0000269|PubMed:24412325};
DE   AltName: Full=UDP-glucose:gallate glucosyltransferase {ECO:0000303|PubMed:24412325};
DE   AltName: Full=Vanillate 1-beta-glucosyltransferase {ECO:0000305};
GN   Name=UGT84A13 {ECO:0000303|PubMed:24412325};
OS   Quercus robur (English oak).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Fagaceae; Quercus.
OX   NCBI_TaxID=38942 {ECO:0000312|EMBL:AHA54051.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC   TISSUE=Flower bud, and Leaf;
RX   PubMed=24412325; DOI=10.1016/j.phytochem.2013.11.023;
RA   Mittasch J., Boettcher C., Frolova N., Boenn M., Milkowski C.;
RT   "Identification of UGT84A13 as a candidate enzyme for the first committed
RT   step of gallotannin biosynthesis in pedunculate oak (Quercus robur).";
RL   Phytochemistry 99:44-51(2014).
CC   -!- FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-
CC       D-glucose esters with hydroxybenzoic acids as preferred glucosyl
CC       acceptors. Has the highest activity with 3,4-dihydroxybenzoate,
CC       vanillate and gallate in vitro. Gallate is the predicted native
CC       substrate of the enzyme, which thus catalyzes the formation of 1-O-
CC       galloyl-beta-D-glucose, the first committed step of gallotannin
CC       biosynthesis. {ECO:0000269|PubMed:24412325}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-
CC         beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834,
CC         ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.136; Evidence={ECO:0000269|PubMed:24412325};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-glucose + vanillate = 1-O-(4-hydroxy-3-
CC         methoxybenzoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:52840,
CC         ChEBI:CHEBI:16632, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC         ChEBI:CHEBI:71512; EC=2.4.1.136;
CC         Evidence={ECO:0000269|PubMed:24412325};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,4-dihydroxybenzoate + UDP-alpha-D-glucose = 1-O-(3,4-
CC         dihydroxy-benzoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:52844,
CC         ChEBI:CHEBI:36241, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC         ChEBI:CHEBI:136876; EC=2.4.1.136;
CC         Evidence={ECO:0000269|PubMed:24412325};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=420 uM for gallate {ECO:0000269|PubMed:24412325};
CC         KM=290 uM for 3,4-dihydroxybenzoate {ECO:0000269|PubMed:24412325};
CC         KM=230 uM for vanillate {ECO:0000269|PubMed:24412325};
CC         Vmax=204 nmol/sec/mg enzyme with gallate as substrate
CC         {ECO:0000269|PubMed:24412325};
CC         Vmax=283 nmol/sec/mg enzyme with 3,4-dihydroxybenzoate as substrate
CC         {ECO:0000269|PubMed:24412325};
CC         Vmax=203 nmol/sec/mg enzyme with vanillate as substrate
CC         {ECO:0000269|PubMed:24412325};
CC   -!- TISSUE SPECIFICITY: Expressed in swelling buds and young leaves.
CC       {ECO:0000269|PubMed:24412325}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KF527849; AHA54051.1; -; mRNA.
DR   AlphaFoldDB; V5LLZ9; -.
DR   SMR; V5LLZ9; -.
DR   KEGG; ag:AHA54051; -.
DR   GO; GO:0047913; F:gallate 1-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
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..510
FT                   /note="Gallate 1-beta-glucosyltransferase"
FT                   /id="PRO_0000440587"
FT   BINDING         340..341
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         358..366
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   510 AA;  56555 MW;  67F500D4483FA55F CRC64;
     MGSEALVHVF LVSFPGQGHV NPLLRLGKRL AAKGLLVTFS TPESIGKQMR KASNITDEPA
     PVGEGFIRFE FFEDGWDEDE PRRQDLDQYL PQLELIGKDI IPKMIRKNAE MGRPVSCLIN
     NPFIPWVSDV AESLGLPSAM LWVQSCACFC AYYHYYHGLV PFPSEAEPFI DIQLPCMPLL
     KYDETPSFLY PTTPYPFLRR AILGQYGNLD KPFCILMDTF QELEHEVIEF MSKICPIKTV
     GPLFKNPKAP NSVRGDFMKA DDCLEWLDSK PPQSVVYISF GSVVYLTQKQ VDEIAFGLLQ
     SGVSFLWVMK PPHKDAGLEL LVLPDGFLEK AGDNGRVVQW SPQEQVLAHP SVACFVTHCG
     WNSTMESLTS GMPVVAFPQW GDQVTDAVYL VDVFKTGVRM CRGEAENRVI TRDEVEKCLL
     EATVGPKAVE MKQNASKWKA AAEAAFSEGG SSDRNIQAFV DEVRARSVAI TGKSTANGVA
     LDLAEKSAEI NGKVDLVETK TNGKVELVEA