Q9LVR1 · U72E2_ARATH
- ProteinUDP-glycosyltransferase 72E2
- GeneUGT72E2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids481 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the O-glucosylation of monolignols (alcohol monomers of lignin) (PubMed:11042211, PubMed:15907484, PubMed:16995900, PubMed:21149736, PubMed:24667164).
Glucosylates coniferyl alcohol to form coniferyl alcohol 4-O-glucoside (PubMed:11042211, PubMed:15907484, PubMed:16995900, PubMed:21149736, PubMed:24667164).
Glucosylates sinapyl alcohol to form sinapyl alcohol 4-O-glucoside (PubMed:11042211, PubMed:12721858, PubMed:15907484, PubMed:21149736, PubMed:24667164).
Glucosylates coniferyl aldehyde to form coniferyl aldehyde 4-O-glucoside (PubMed:15907484).
Glucosylates sinapyl aldehyde to form sinapyl aldehyde 4-O-glucoside (PubMed:15907484).
Possesses low activity with sinapate and ferulate as substrates (PubMed:11042211, PubMed:15907484).
Glucosylates coniferyl alcohol to form coniferyl alcohol 4-O-glucoside (PubMed:11042211, PubMed:15907484, PubMed:16995900, PubMed:21149736, PubMed:24667164).
Glucosylates sinapyl alcohol to form sinapyl alcohol 4-O-glucoside (PubMed:11042211, PubMed:12721858, PubMed:15907484, PubMed:21149736, PubMed:24667164).
Glucosylates coniferyl aldehyde to form coniferyl aldehyde 4-O-glucoside (PubMed:15907484).
Glucosylates sinapyl aldehyde to form sinapyl aldehyde 4-O-glucoside (PubMed:15907484).
Possesses low activity with sinapate and ferulate as substrates (PubMed:11042211, PubMed:15907484).
Miscellaneous
Plants overexpressing UGT72E2 show increased accumulation of monolignol glucosides in roots and appearance of these glucosides in leaves.
Catalytic activity
- (E)-4-coumarate + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-trans-4-coumarate + H+ + UDP
- (E)-sinapyl alcohol + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-trans-4-sinapoyl alcohol + H+ + UDP
- (E)-sinapate + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-trans-sinapate + H+ + UDP
- (E)-coniferaldehyde + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-4-(E)-coniferyl aldehyde + H+ + UDP
- (E)-sinapaldehyde + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-4-trans-sinapoyl aldehyde + H+ + UDP
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
20 μM | coniferyl aldehyde | |||||
20 μM | sinapyl aldehyde | |||||
60 μM | coniferyl alcohol | |||||
150 μM | sinapyl alcohol | |||||
260 μM | coniferyl alcohol | |||||
240 μM | sinapyl alcohol | |||||
450 μM | ferulate | |||||
900 μM | sinapate |
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 18 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 18 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 111 | Charge relay | ||||
Sequence: D | ||||||
Binding site | 346 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 348 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 363 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 366 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 368 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 371 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 386 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 387 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 388 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | coniferyl-alcohol glucosyltransferase activity | |
Molecular Function | daphnetin 4-O-beta-glucosyltransferase activity | |
Molecular Function | esculetin 4-O-beta-glucosyltransferase activity | |
Molecular Function | hydroxycinnamate 4-beta-glucosyltransferase activity | |
Molecular Function | UDP-glucose:coniferaldehyde 4-beta-D-glucosyltransferase activity | |
Molecular Function | UDP-glucose:sinapaldehyde 4-beta-D-glucosyltransferase activity | |
Biological Process | lignin metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUDP-glycosyltransferase 72E2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9LVR1
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000409074 | 1-481 | UDP-glycosyltransferase 72E2 | |||
Sequence: MHITKPHAAMFSSPGMGHVIPVIELGKRLSANNGFHVTVFVLETDAASAQSKFLNSTGVDIVKLPSPDIYGLVDPDDHVVTKIGVIMRAAVPALRSKIAAMHQKPTALIVDLFGTDALCLAKEFNMLSYVFIPTNARFLGVSIYYPNLDKDIKEEHTVQRNPLAIPGCEPVRFEDTLDAYLVPDEPVYRDFVRHGLAYPKADGILVNTWEEMEPKSLKSLLNPKLLGRVARVPVYPIGPLCRPIQSSETDHPVLDWLNEQPNESVLYISFGSGGCLSAKQLTELAWGLEQSQQRFVWVVRPPVDGSCCSEYVSANGGGTEDNTPEYLPEGFVSRTSDRGFVVPSWAPQAEILSHRAVGGFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALLSDELGIAVRLDDPKEDISRWKIEALVRKVMTEKEGEAMRRKVKKLRDSAEMSLSIDGGGLAHESLCRVTKECQRFLERVVDLSRGA |
Proteomic databases
Expression
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length481
- Mass (Da)52,992
- Last updated2000-10-01 v1
- ChecksumEE46B76C4BD14745
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 4; AAM62659 | ||||
Sequence: I → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018119 EMBL· GenBank· DDBJ | BAA97275.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED98252.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY062636 EMBL· GenBank· DDBJ | AAL32714.1 EMBL· GenBank· DDBJ | mRNA | ||
AY064651 EMBL· GenBank· DDBJ | AAL47362.1 EMBL· GenBank· DDBJ | mRNA | ||
AY085432 EMBL· GenBank· DDBJ | AAM62659.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |