GGT24_PUNGR
ID GGT24_PUNGR Reviewed; 517 AA.
AC A0A193AU77;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Gallate 1-beta-glucosyltransferase 84A24 {ECO:0000305};
DE EC=2.4.1.136 {ECO:0000269|PubMed:27227328};
DE AltName: Full=UDP-glucose:gallate glucosyltransferase {ECO:0000305};
DE AltName: Full=UDP-glycosyltransferase 84A24 {ECO:0000303|PubMed:27227328};
DE EC=2.4.1.120 {ECO:0000269|PubMed:27227328};
DE EC=2.4.1.170 {ECO:0000269|PubMed:27227328};
DE EC=2.4.1.177 {ECO:0000269|PubMed:27227328};
DE EC=2.4.1.194 {ECO:0000269|PubMed:27227328};
DE EC=2.4.1.81 {ECO:0000269|PubMed:27227328};
GN Name=UGT84A24 {ECO:0000303|PubMed:27227328, ECO:0000312|EMBL:ANN02877.1};
GN ORFNames=CRG98_007995 {ECO:0000312|EMBL:PKI71672.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000312|EMBL:ANN02877.1};
RN [1] {ECO:0000312|EMBL:ANN02877.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27227328; DOI=10.1371/journal.pone.0156319;
RA Ono N.N., Qin X., Wilson A.E., Li G., Tian L.;
RT "Two UGT84 Family Glycosyltransferases Catalyze a Critical Reaction of
RT Hydrolyzable Tannin Biosynthesis in Pomegranate (Punica granatum).";
RL PLoS ONE 11:E0156319-E0156319(2016).
RN [2] {ECO:0000312|EMBL:PKI71672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AG2017; TISSUE=Leaf {ECO:0000312|EMBL:PKI71672.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-
CC D-glucose esters with hydroxybenzoic acids and cinnamic acid including
CC its derivatives as preferred glucosyl acceptors. Has significant
CC activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-
CC dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic
CC acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic
CC acid is the predicted native substrate of the enzyme, which thus
CC catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first
CC committed step of hydrolyzable tannins (HTs) biosynthesis, with
CC punicalagin isomers being the major HTs of pomegranate. Catalyzes the
CC formation of flavonoid glucosides with genistein, apigenin and luteolin
CC in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-
CC hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and
CC quercetin. No activity with catechol, resveratrol, chlorogenic acid,
CC catechin and epicatechin (building blocks of proanthocyanidins) or
CC cyanidin, delphinidin and pelargonidin (the three anthocyanidins).
CC {ECO:0000269|PubMed:27227328}.
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:27227328};
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:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + UDP-alpha-D-glucose = 4-(beta-D-
CC glucosyloxy)benzoate + H(+) + UDP; Xref=Rhea:RHEA:15153,
CC ChEBI:CHEBI:11935, ChEBI:CHEBI:15378, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.194;
CC Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-
CC beta-D-glucose + UDP; Xref=Rhea:RHEA:13437, ChEBI:CHEBI:15669,
CC ChEBI:CHEBI:16279, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.177; Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=E-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-
CC D-glucose + UDP; Xref=Rhea:RHEA:13305, ChEBI:CHEBI:16546,
CC ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.120; Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + UDP-alpha-D-glucose = 1-O-(trans-4-
CC coumaroyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:57472,
CC ChEBI:CHEBI:12876, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:71498; Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeate + UDP-alpha-D-glucose = 1-O-[(E)-caffeoyl]-beta-
CC D-glucose + UDP; Xref=Rhea:RHEA:57464, ChEBI:CHEBI:614,
CC ChEBI:CHEBI:57770, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-ferulate + UDP-alpha-D-glucose = 1-O-[(E)-feruloyl]-beta-
CC D-glucose + UDP; Xref=Rhea:RHEA:57468, ChEBI:CHEBI:29749,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:81321;
CC Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=genistein + UDP-alpha-D-glucose = genistein 7-O-beta-D-
CC glucoside + H(+) + UDP; Xref=Rhea:RHEA:56056, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:74224,
CC ChEBI:CHEBI:140305; EC=2.4.1.170;
CC Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apigenin + UDP-alpha-D-glucose = apigenin 7-O-beta-D-glucoside
CC + H(+) + UDP; Xref=Rhea:RHEA:59760, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58470, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:77722; EC=2.4.1.81;
CC Evidence={ECO:0000269|PubMed:27227328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=luteolin + UDP-alpha-D-glucose = H(+) + luteolin 7-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:19577, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57545, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:77791; EC=2.4.1.81;
CC Evidence={ECO:0000269|PubMed:27227328};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.98 mM for gallic acid (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27227328};
CC KM=1.17 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:27227328};
CC KM=4.44 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:27227328};
CC KM=1.77 mM for caffeic acid (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27227328};
CC KM=0.86 mM for cinnamic acid (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27227328};
CC KM=1.06 mM for coumaric acid (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27227328};
CC KM=1.32 mM for ferulic acid (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27227328};
CC KM=0.78 mM for sinapic acid (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27227328};
CC Vmax=0.39 uM/sec/mg enzyme with gallic acid as substrate (at pH 5.0
CC and 30 degrees Celsius);
CC Vmax=0.43 uM/sec/mg enzyme with 4-hydroxybenzoic acid as substrate
CC (at pH 5.0 and 30 degrees Celsius);
CC Vmax=0.96 uM/sec/mg enzyme with 3,4-dihydroxybenzoic acid as
CC substrate (at pH 5.0 and 30 degrees Celsius);
CC Vmax=0.63 uM/sec/mg enzyme with caffeic acid as substrate (at pH 5.0
CC and 30 degrees Celsius);
CC Vmax=0.32 uM/sec/mg enzyme with cinnamic acid as substrate (at pH 5.0
CC and 30 degrees Celsius);
CC Vmax=0.31 uM/sec/mg enzyme with coumaric acid as substrate (at pH 5.0
CC and 30 degrees Celsius);
CC Vmax=0.47 uM/sec/mg enzyme with ferulic acid as substrate (at pH 5.0
CC and 30 degrees Celsius);
CC Vmax=0.31 uM/sec/mg enzyme with sinapic acid as substrate (at pH 5.0
CC and 30 degrees Celsius);
CC Note=kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6
CC sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1)
CC with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1)
CC with caffeic acid as substrate. kcat is 0.45 sec(-1) with cinnamic
CC acid as substrate. kcat is 0.44 sec(-1) with coumaric acid as
CC substrate. kcat is 0.66 sec(-1) with ferulic acid as substrate. kcat
CC is 0.44 sec(-1) with sinapic acid as substrate.
CC {ECO:0000269|PubMed:27227328};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:27227328};
CC Temperature dependence:
CC Activity remains fairly constant between 20-55 degrees Celsius.
CC Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaf. Also expressed in peel,
CC stem, root and aril. {ECO:0000269|PubMed:27227328}.
CC -!- DISRUPTION PHENOTYPE: No difference in the levels of punicalagin in
CC pomegranate hairy roots in a single RNAi knockdown of this gene.
CC However, double RNAi knockdown of this gene together with UGT84A23
CC leads to significantly reduced levels of punicalagin and bis-
CC hexahydroxydipheynyl glucose isomers, and to increased levels of
CC galloyl glucosides (ether-linked gallic acid and glucose).
CC {ECO:0000269|PubMed:27227328}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000255|RuleBase:RU003718}.
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DR EMBL; KT159807; ANN02877.1; -; mRNA.
DR EMBL; PGOL01000363; PKI71672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A193AU77; -.
DR SMR; A0A193AU77; -.
DR STRING; 22663.A0A193AU77; -.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000233551; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0047250; F:4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050412; F:cinnamate beta-D-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047891; F:flavone 7-O-beta-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047913; F:gallate 1-beta-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050004; F:isoflavone 7-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050284; F:sinapate 1-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046278; P:3,4-dihydroxybenzoate metabolic process; IDA:UniProtKB.
DR GO; GO:0009801; P:cinnamic acid ester metabolic process; IDA:UniProtKB.
DR GO; GO:0033494; P:ferulate metabolic process; 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 Cytoplasm; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..517
FT /note="Gallate 1-beta-glucosyltransferase 84A24"
FT /id="PRO_0000452359"
FT BINDING 283
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 341..342
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 359..367
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 381..384
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ SEQUENCE 517 AA; 57277 MW; 79D530B673809A51 CRC64;
MGSESLVHVF LVSFPGQGHV NPLLRLGKRL ASKGLLVTFT TPESIGKQMR KASNIGEEPS
PIGDGFIRFE FFEDGWDEDE PRRQDLDQYL PQLEKVGKEV IPRMIKKNEE QNRPVSCLIN
NPFIPWVSDV AESLGLPSAM LWVQSCACFA AYYHYYHGLV PFPSESAMEI DVQLPCMPLL
KHDEVPSFLY PTTPYPFLRR AIMGQYKNLD KPFCVLMDTF QELEHEIIEY MSKICPIKTV
GPLFKNPKAP NANVRGDFMK ADDCISWLDS KPPASVVYVS FGSVVYLKQD QWDEIAFGLL
NSGLNFLWVM KPPHKDSGYQ LLTLPEGFLE KAGDKGKVVQ WSPQEQVLAH PSVACFVTHC
GWNSSMEALS SGMPVVAFPQ WGDQVTDAKY LVDVFKVGVR MCRGEAENKL IMRDVVEKCL
LEATVGPKAA EVKENALKWK AAAEAAVAEG GSSDRNIQAF VDEVKRRSIA IQSNKSEPKP
VVQNAAVADH FGAKATTNGV AADLAGSNAD GKVELVA
