Q9SBL1 · HMNGT_SORBI
- ProteinCyanohydrin beta-glucosyltransferase
- GeneUGT85B1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids492 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthesis of the cyanogenic glucoside dhurrin. Prevents the dissociation and release of toxic hydrogen cyanide. Mandelonitrile, p-hydroxymandelonitrile, benzyl alcohol, benzoic acid and geraniol, but not hydroquinone(1,4-benzenediol), alpha-terpinol, linalool or farnesol are utilized as acceptor substrates. UDP-glucose, but not UDP-xylose or UDP-glucuronic acid can be used as sugar donor.
Catalytic activity
- (S)-4-hydroxymandelonitrile + UDP-alpha-D-glucose = dhurrin + H+ + UDP
Activity regulation
Inhibited by p-hydroxybenzaldehyde.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.14 mM | geraniol | |||||
0.13 mM | beta-citronellol | |||||
1.13 mM | nerol | |||||
0.66 mM | 1-hexanol | |||||
0.73 mM | cis-3-hexen-1-ol | |||||
0.84 mM | mandelonitrile | |||||
6.33 mM | 2-hydroxy-3-methoxybenzyl alcohol | |||||
0.69 mM | 3-methyl-3-buten-1-ol | |||||
10.3 mM | 3-methyl-2-buten-1-ol | |||||
0.8 mM | UDP-glucose |
Pathway
Secondary metabolite biosynthesis; dhurrin biosynthesis; dhurrin from L-tyrosine: step 3/3.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 23 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 23 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 130 | Charge relay | ||||
Sequence: D | ||||||
Binding site | 152 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 371 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 386 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 389 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 390 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 391 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 394 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 409 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 410 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 411 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | cyanohydrin beta-glucosyltransferase activity | |
Biological Process | dhurrin biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCyanohydrin beta-glucosyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Sorghinae > Sorghum
Accessions
- Primary accessionQ9SBL1
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Peripheral membrane protein
Note: In the presence of CYP79A1 and CYP71E1, moves toward the surface of the ER membranes in order to form a metabolon.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 201 | 20-fold reduction in activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 391 | 185-fold reduction in activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 410 | 225-fold reduction in activity. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000365608 | 1-492 | Cyanohydrin beta-glucosyltransferase | |||
Sequence: MGSNAPPPPTPHVVLVPFPGQGHVAPLMQLARLLHARGARVTFVYTQYNYRRLLRAKGEAAVRPPATSSARFRIEVIDDGLSLSVPQNDVGGLVDSLRKNCLHPFRALLRRLGQEVEGQDAPPVTCVVGDVVMTFAAAAAREAGIPEVQFFTASACGLLGYLHYGELVERGLVPFRDASLLADDDYLDTPLEWVPGMSHMRLRDMPTFCRTTDPDDVMVSATLQQMESAAGSKALILNTLYELEKDVVDALAAFFPPIYTVGPLAEVIASSDSASAGLAAMDISIWQEDTRCLSWLDGKPAGSVVYVNFGSMAVMTAAQAREFALGLASCGSPFLWVKRPDVVEGEEVLLPEALLDEVARGRGLVVPWCPQAAVLKHAAVGLFVSHCGWNSLLEATAAGQPVLAWPCHGEQTTNCRQLCEVWGNGAQLPREVESGAVARLVREMMVGDLGKEKRAKAAEWKAAAEAAARKGGASWRNVERVVNDLLLVGGKQ |
Post-translational modification
The N-terminus is partially blocked.
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length492
- Mass (Da)52,916
- Last updated2000-05-01 v1
- ChecksumABC6A57AC51E9BE7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF199453 EMBL· GenBank· DDBJ | AAF17077.1 EMBL· GenBank· DDBJ | mRNA |