A0A2S1XB67 · ASO_CATRO
- ProteinO-acetylstemmadenine oxidase
- GeneASO
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids529 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts O-acetylstemmadenine (OAS) to reactive acetylated intermediates, likely dihydroprecondylocarpine acetate.
Catalytic activity
- O-acetyl-15alpha-stemmadenine + O2 = H2O2 + precondylocarpine acetateThis reaction proceeds in the forward direction.
Cofactor
Pathway
Alkaloid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 102-108 | FAD (UniProtKB | ChEBI) | ||||
Sequence: IRSGGAD | ||||||
Binding site | 113 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 168-169 | FAD (UniProtKB | ChEBI) | ||||
Sequence: VS | ||||||
Binding site | 173-177 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GIGGH | ||||||
Binding site | 183 | FAD (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 465 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | vacuole | |
Cellular Component | vesicle | |
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | alkaloid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameO-acetylstemmadenine oxidase
- EC number
- Short namesCrASO
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Gentianales > Apocynaceae > Rauvolfioideae > Vinceae > Catharanthinae > Catharanthus
Accessions
- Primary accessionA0A2S1XB67
Subcellular Location
UniProt Annotation
GO Annotation
Note: First targeted to endoplasmic reticulum (ER) and progressively secreted to vacuole by ER-derived vesicles.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Accumulates O-acetylstemmadenine (OAS) at the expense of catharanthine and vindoline (PubMed:29724909, PubMed:30256480).
Strong accumulation of stemmadenine acetate (PubMed:29724909).
Strong accumulation of stemmadenine acetate (PubMed:29724909).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 188 | Very low enzyme activity leading to the accumulation of O-acetylstemmadenine (OAS) at the expense of catharanthine, vindoline and vindorosine. | ||||
Sequence: R → W |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MIKKVPIVLSIFCFLLLLSSSHG | ||||||
Chain | PRO_5015696778 | 24-529 | O-acetylstemmadenine oxidase | |||
Sequence: SIPEAFLNCISNKFSLDVSILNILHVPSNSSYDSVLKSTIQNPRFLKSPKPLAIITPVLHSHVQSAVICTKQAGLQIRIRSGGADYEGLSYRSEVPFILLDLQNLRSISVDIEDNSAWVESGATIGEFYHEIAQNSPVHAFPAGVSSSVGIGGHLSSGGFGTLLRKYGLAADNIIDAKIVDARGRILDRESMGEDLFWAIRGGGGASFGVIVSWKVKLVKVPPMVTVFILSKTYEEGGLDLLHKWQYIEHKLPEDLFLAVSIMDDSSSGNKTLMAGFMSLFLGKTEDLLKVMAENFPQLGLKKEDCLEMNWIDAAMYFSGHPIGESRSVLKNRESHLPKTCVSIKSDFIQEPQSMDALEKLWKFCREEENSPIILMLPLGGMMSKISESEIPFPYRKDVIYSMIYEIVWNCEDDESSEEYIDGLGRLEELMTPYVKQPRGSWFSTRNLYTGKNKGPGTTYSKAKEWGFRYFNNNFKKLALIKGQVDPENFFYYEQSIPPLHLQVEL | ||||||
Disulfide bond | 32↔92 | |||||
Sequence: CISNKFSLDVSILNILHVPSNSSYDSVLKSTIQNPRFLKSPKPLAIITPVLHSHVQSAVIC | ||||||
Glycosylation | 52 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 293 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed in leaf epidermis.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 70-244 | FAD-binding PCMH-type | ||||
Sequence: KSPKPLAIITPVLHSHVQSAVICTKQAGLQIRIRSGGADYEGLSYRSEVPFILLDLQNLRSISVDIEDNSAWVESGATIGEFYHEIAQNSPVHAFPAGVSSSVGIGGHLSSGGFGTLLRKYGLAADNIIDAKIVDARGRILDRESMGEDLFWAIRGGGGASFGVIVSWKVKLVKV |
Sequence similarities
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length529
- Mass (Da)59,214
- Last updated2018-07-18 v1
- Checksum7B362368349F3B53