A0A193AU77 · GGT24_PUNGR

  • Protein
    Gallate 1-beta-glucosyltransferase 84A24
  • Gene
    UGT84A24
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.98 mMgallic acid5.030
1.17 mM4-hydroxybenzoic acid5.030
4.44 mM3,4-dihydroxybenzoic acid5.030
1.77 mMcaffeic acid5.030
0.86 mMcinnamic acid5.030
1.06 mMcoumaric acid5.030
1.32 mMferulic acid5.030
0.78 mMsinapic acid5.030
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
0.39 μM/sec/mg5.030with gallic acid as substrate
0.43 μM/sec/mg5.030with 4-hydroxybenzoic acid as substrate
0.96 μM/sec/mg5.030with 3,4-dihydroxybenzoic acid as substrate
0.63 μM/sec/mg5.030with caffeic acid as substrate
0.32 μM/sec/mg5.030with cinnamic acid as substrate
0.31 μM/sec/mg5.030with coumaric acid as substrate
0.47 μM/sec/mg5.030with ferulic acid as substrate
0.31 μM/sec/mg5.030with 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.

TypeIDPosition(s)Description
Active site19Proton acceptor
Binding site19an anthocyanidin (UniProtKB | ChEBI)
Binding site344UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site359UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site362UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site363UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site364UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site367UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site382an anthocyanidin (UniProtKB | ChEBI)
Binding site383UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site384UDP-alpha-D-glucose (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity
Molecular Functioncinnamate beta-D-glucosyltransferase activity
Molecular Functionflavone 7-O-beta-glucosyltransferase activity
Molecular Functiongallate 1-beta-glucosyltransferase activity
Molecular Functionisoflavone 7-O-glucosyltransferase activity
Molecular Functionquercetin 3-O-glucosyltransferase activity
Molecular Functionquercetin 7-O-glucosyltransferase activity
Molecular Functionsinapate 1-glucosyltransferase activity
Molecular FunctionUDP-glucosyltransferase activity
Biological Process3,4-dihydroxybenzoate metabolic process
Biological Processcinnamic acid ester metabolic process
Biological Processferulate metabolic process

Keywords

Enzyme and pathway databases

Community curation (1)

Community annotation

Glucoside/glucose ester-forming activities with various hydroxybenzoic acids, hydroxycinnamic acids, and flavonoids.

SourceSubmission dateContributor
PubMed:272273280000-0002-0431-4037

Names & Taxonomy

Protein names

  • Recommended name
    Gallate 1-beta-glucosyltransferase 84A24
  • EC number
  • Alternative names
    • UDP-glucose:gallate glucosyltransferase
    • UDP-glycosyltransferase 84A24
      (EC:2.4.1.120
      , EC:2.4.1.170
      , EC:2.4.1.177
      , EC:2.4.1.194
      , EC:2.4.1.81
      ) . EC:2.4.1.120 (UniProtKB | ENZYME | Rhea)
      , EC:2.4.1.170 (UniProtKB | ENZYME | Rhea)
      , EC:2.4.1.177 (UniProtKB | ENZYME | Rhea)
      , EC:2.4.1.194 (UniProtKB | ENZYME | Rhea)
      , EC:2.4.1.81 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      UGT84A24
    • ORF names
      CRG98_007995

Organism names

  • Taxonomic identifier
  • Strain
    • cv. AG2017
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Myrtales > Lythraceae > Punica

Accessions

  • Primary accession
    A0A193AU77

Proteomes

Subcellular Location

Keywords

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.

TypeIDPosition(s)Description
ChainPRO_00004523591-517Gallate 1-beta-glucosyltransferase 84A24

Expression

Tissue specificity

Highly expressed in leaf. Also expressed in peel, stem, root and aril.

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    517
  • Mass (Da)
    57,277
  • Last updated
    2016-10-05 v1
  • Checksum
    79D530B673809A51
MGSESLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNIGEEPSPIGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKEVIPRMIKKNEEQNRPVSCLINNPFIPWVSDVAESLGLPSAMLWVQSCACFAAYYHYYHGLVPFPSESAMEIDVQLPCMPLLKHDEVPSFLYPTTPYPFLRRAIMGQYKNLDKPFCVLMDTFQELEHEIIEYMSKICPIKTVGPLFKNPKAPNANVRGDFMKADDCISWLDSKPPASVVYVSFGSVVYLKQDQWDEIAFGLLNSGLNFLWVMKPPHKDSGYQLLTLPEGFLEKAGDKGKVVQWSPQEQVLAHPSVACFVTHCGWNSSMEALSSGMPVVAFPQWGDQVTDAKYLVDVFKVGVRMCRGEAENKLIMRDVVEKCLLEATVGPKAAEVKENALKWKAAAEAAVAEGGSSDRNIQAFVDEVKRRSIAIQSNKSEPKPVVQNAAVADHFGAKATTNGVAADLAGSNADGKVELVA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KT159807
EMBL· GenBank· DDBJ
ANN02877.1
EMBL· GenBank· DDBJ
mRNA
PGOL01000363
EMBL· GenBank· DDBJ
PKI71672.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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