A0A193AU77 · GGT24_PUNGR
- ProteinGallate 1-beta-glucosyltransferase 84A24
- GeneUGT84A24
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids517 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins).
Catalytic activity
- 3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP
- (E)-4-coumarate + UDP-alpha-D-glucose = 1-O-(trans-4-coumaroyl)-beta-D-glucose + UDP
- (E)-caffeate + UDP-alpha-D-glucose = 1-O-[(E)-caffeoyl]-beta-D-glucose + UDP
- (E)-ferulate + UDP-alpha-D-glucose = 1-O-[(E)-feruloyl]-beta-D-glucose + UDP
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.98 mM | gallic acid | 5.0 | 30 | |||
1.17 mM | 4-hydroxybenzoic acid | 5.0 | 30 | |||
4.44 mM | 3,4-dihydroxybenzoic acid | 5.0 | 30 | |||
1.77 mM | caffeic acid | 5.0 | 30 | |||
0.86 mM | cinnamic acid | 5.0 | 30 | |||
1.06 mM | coumaric acid | 5.0 | 30 | |||
1.32 mM | ferulic acid | 5.0 | 30 | |||
0.78 mM | sinapic acid | 5.0 | 30 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.39 μM/sec/mg | 5.0 | 30 | with gallic acid as substrate | ||
0.43 μM/sec/mg | 5.0 | 30 | with 4-hydroxybenzoic acid as substrate | ||
0.96 μM/sec/mg | 5.0 | 30 | with 3,4-dihydroxybenzoic acid as substrate | ||
0.63 μM/sec/mg | 5.0 | 30 | with caffeic acid as substrate | ||
0.32 μM/sec/mg | 5.0 | 30 | with cinnamic acid as substrate | ||
0.31 μM/sec/mg | 5.0 | 30 | with coumaric acid as substrate | ||
0.47 μM/sec/mg | 5.0 | 30 | with ferulic acid as substrate | ||
0.31 μM/sec/mg | 5.0 | 30 | with sinapic acid as substrate |
kcat is 0.55 sec-1 with gallic acid as substrate. kcat is 0.6 sec-1 with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec-1 with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec-1 with caffeic acid as substrate. kcat is 0.45 sec-1 with cinnamic acid as substrate. kcat is 0.44 sec-1 with coumaric acid as substrate. kcat is 0.66 sec-1 with ferulic acid as substrate. kcat is 0.44 sec-1 with sinapic acid as substrate.
pH Dependence
Optimum pH is 4.5.
Temperature Dependence
Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 19 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 19 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 344 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 359 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 362 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 363 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 364 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 367 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 382 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 383 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 384 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity | |
Molecular Function | cinnamate beta-D-glucosyltransferase activity | |
Molecular Function | flavone 7-O-beta-glucosyltransferase activity | |
Molecular Function | gallate 1-beta-glucosyltransferase activity | |
Molecular Function | isoflavone 7-O-glucosyltransferase activity | |
Molecular Function | quercetin 3-O-glucosyltransferase activity | |
Molecular Function | quercetin 7-O-glucosyltransferase activity | |
Molecular Function | sinapate 1-glucosyltransferase activity | |
Molecular Function | UDP-glucosyltransferase activity | |
Biological Process | 3,4-dihydroxybenzoate metabolic process | |
Biological Process | cinnamic acid ester metabolic process | |
Biological Process | ferulate metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Community annotation
Glucoside/glucose ester-forming activities with various hydroxybenzoic acids, hydroxycinnamic acids, and flavonoids.
Source | Submission date | Contributor |
---|---|---|
PubMed:27227328 | 0000-0002-0431-4037 |
Names & Taxonomy
Protein names
- Recommended nameGallate 1-beta-glucosyltransferase 84A24
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Myrtales > Lythraceae > Punica
Accessions
- Primary accessionA0A193AU77
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No difference in the levels of punicalagin in pomegranate hairy roots in a single RNAi knockdown of this gene. However, double RNAi knockdown of this gene together with UGT84A23 leads to significantly reduced levels of punicalagin and bis-hexahydroxydipheynyl glucose isomers, and to increased levels of galloyl glucosides (ether-linked gallic acid and glucose).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452359 | 1-517 | Gallate 1-beta-glucosyltransferase 84A24 | |||
Sequence: MGSESLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNIGEEPSPIGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKEVIPRMIKKNEEQNRPVSCLINNPFIPWVSDVAESLGLPSAMLWVQSCACFAAYYHYYHGLVPFPSESAMEIDVQLPCMPLLKHDEVPSFLYPTTPYPFLRRAIMGQYKNLDKPFCVLMDTFQELEHEIIEYMSKICPIKTVGPLFKNPKAPNANVRGDFMKADDCISWLDSKPPASVVYVSFGSVVYLKQDQWDEIAFGLLNSGLNFLWVMKPPHKDSGYQLLTLPEGFLEKAGDKGKVVQWSPQEQVLAHPSVACFVTHCGWNSSMEALSSGMPVVAFPQWGDQVTDAKYLVDVFKVGVRMCRGEAENKLIMRDVVEKCLLEATVGPKAAEVKENALKWKAAAEAAVAEGGSSDRNIQAFVDEVKRRSIAIQSNKSEPKPVVQNAAVADHFGAKATTNGVAADLAGSNADGKVELVA |
Expression
Tissue specificity
Highly expressed in leaf. Also expressed in peel, stem, root and aril.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length517
- Mass (Da)57,277
- Last updated2016-10-05 v1
- Checksum79D530B673809A51
Keywords
- Technical term