B2XBQ5 · 85A19_PRUDU
- Protein(R)-mandelonitrile beta-glucosyltransferase
- GeneUGT85A19
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids483 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Involved in the biosynthesis of the cyanogenic glycoside (R)-prunasin, a precursor of (R)-amygdalin, which at high concentrations is associated with intense bitterness in kernels of almond (PubMed:32688778).
Stereo-selectively glucosylates (R)-mandelonitrile to produce (R)-prunasin (PubMed:32688778).
Stereo-selectively glucosylates (R)-mandelonitrile to produce (R)-prunasin (PubMed:32688778).
Catalytic activity
- (R)-mandelonitrile + UDP-alpha-D-glucose = (R)-prunasin + H+ + UDPThis reaction proceeds in the forward direction.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 22 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 22 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 124 | Charge relay | ||||
Sequence: D | ||||||
Binding site | 146 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 363 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 378 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 381 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 382 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 383 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 386 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 401 | an anthocyanidin (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 402 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 403 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | UDP-glycosyltransferase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended name(R)-mandelonitrile beta-glucosyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus
Accessions
- Primary accessionB2XBQ5
- Secondary accessions
Proteomes
Genome annotation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451484 | 1-483 | (R)-mandelonitrile beta-glucosyltransferase | |||
Sequence: MSPVASKEKPHAVFVPFPAQGHINPMLQLAKLLNYKGFHITFVNTEFNHKRMLESQGSHALDGLPSFRFETIPDGLPPADADARRNLPLVCDSTSKTCLAPFEALLTKLNSSPDSPPVTCIVADGVTSFTLDAAEHFGIPEVLFWTTSACGLMGYVQYYRLIEKGLTPFKDAKDFANGYLDTEIDWIPGMKDVRLKDMPSFIRTTDPNDIMLHYMVSETERSKKASAIILNTFDALEQEVVDALSTLLPPIYSIGPLQLPYSEIPSEYNDLKAIGSNLWAENTECLNWLDTKEPNSVVYVNFGSTTVMTNEQLVEFSWGLANSKKPFLWIIRPGLVAGETAVVPPEFLEETKERGMLASWCPQEQVLLHSAIGGFLTHSGWNSTLEALCGGVPLICWPFFAEQQTNVRYSCTQWGIGIEIDGEVKRDYIDGLVRTLMDGEEGKKMRKKALEWKMLAEDATAPKGSSYLALENVVSKVLLSPRD |
Structure
Sequence
- Sequence statusComplete
- Length483
- Mass (Da)53,697
- Last updated2020-12-02 v2
- Checksum2B6252C85CB4F203
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 127 | in Ref. 1; ABV68925 | ||||
Sequence: T → S | ||||||
Sequence conflict | 454 | in Ref. 1; ABV68925 | ||||
Sequence: M → K | ||||||
Sequence conflict | 461 | in Ref. 1; ABV68925 | ||||
Sequence: A → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EU015987 EMBL· GenBank· DDBJ | ABV68925.1 EMBL· GenBank· DDBJ | mRNA | ||
CABIKO010000198 EMBL· GenBank· DDBJ | VVA30855.1 EMBL· GenBank· DDBJ | Genomic DNA |