Q9ZP27 · AVCO2_AVESA
- ProteinAvenacosidase 2
- GeneP60B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids578 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Beta-glucosidase acting as a preformed defense system. Hydrolyzes the bisdesmosides avenacosides A and B to 26-desgluco-avenacosides exhibiting fungicidal activity. Can use beta-fucoside > beta-glucoside > beta-galactoside > beta-xyloside as substrates, but not alpha-glycosides, beta-thioglucosides and disaccharides (By similarity).
Catalytic activity
- avenacoside B + H2O = 26-desgluco-avenacoside B + D-glucose
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.48 mM | p-nitrophenyl-beta-D-glucopyranoside | with heteromultimeric recombinant enzyme | ||||
2.47 mM | p-nitrophenyl-beta-D-glucopyranoside | with homodimeric recombinant enzyme |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 89 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 193 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 238-239 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: NE | ||||||
Active site | 239 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 381 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 454 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 454 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 504 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 511-512 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: EW | ||||||
Binding site | 520 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Molecular Function | beta-glucosidase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | defense response |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAvenacosidase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Poodae > Poeae > Poeae Chloroplast Group 1 (Aveneae type) > Aveninae > Avena
Accessions
- Primary accessionQ9ZP27
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in a fibrillar spherulite called stromacentre.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-57 | Chloroplast | ||||
Sequence: MALLCSALSNSTHPSFRSHIAGANSENLWHLSAHPAQKSKRRCNLTLSSRAAARISS | ||||||
Chain | PRO_0000428641 | 58-578 | Avenacosidase 2 | |||
Sequence: ALESGKLKPWQIPKRDWFPPEFTFGAASAAYQIEGAWNEGGKGPSSWDNFCHNYPERIMDGSNWDVAANSYYMYKEDVRMLKEIGMDSYRFSISWPRILPEGTLEGGINHEGIQYYNDLLDCLIENGIKPYITLFHWDTPQALADKYNDFLDRRIVKDYTDYATVCFEHFGDKVKNWITFNEPHSFCGLAYGTGLHAPGLCSPGMDCAIPQGDALRQPYIVGHNLLLAHAETVDVYKKFYKGDDGQIGMVMDVMAYEPYGNNFVDQQAQERSIDFHIGWFLEPMVRGDYPFSMRSLVGDRLPFFTKSEQEKLVSSYDFVGINYYTARFSEHIDISPEIIPKLNTDDAYSTPEFNDSNGIPIGPDLGMYWILSYPKGLKDILLLMKEKYGNPPIYITENGTADMDGWGNPPMTDPLDDPLRIEYLQQHMTAIKEAIDLGADVRGHFTWSLIDNFEWSMGYLSRFGIVYIDRNDGFKRIMKKSAKWLKEFNGATKEVNNKILGASSCCSGELMWFLVQNPYGK | ||||||
Disulfide bond | 258↔264 | |||||
Sequence: CSPGMDC |
Keywords
- PTM
Interaction
Subunit
Heteromultimer with P60A in a 1:1 stoichiometry. Aggregates to form the fibrillar stromacentre.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length578
- Mass (Da)65,693
- Last updated1999-05-01 v1
- ChecksumFA800D307BAEB7E8
Keywords
- Technical term