B9RVF8 · B9RVF8_RICCO
- Proteinperoxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids264 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic activity
- 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 calcium ions per subunit.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 7 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 11 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 12 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 15 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 17 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 19 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 21 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 34 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 109 | substrate | ||||
Sequence: P | ||||||
Binding site | 139 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 140 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 184 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 192 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | heme binding | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameperoxidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Malpighiales > Euphorbiaceae > Acalyphoideae > Acalypheae > Ricinus
Accessions
- Primary accessionB9RVF8
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 13↔18 | |||||
Sequence: CFVNGC | ||||||
Disulfide bond | 67↔260 | |||||
Sequence: CADILAVAARDSVVALGGPSWQVELGRRDSTTASYDAANTDLPSPLMDLSDLISALSRKGFTAKEMVALAGSHTIGQARCLMFRGRLYNETNIDSALATSLKSDCPTTGSDDNLSPLDATSPVIFDNSYFKNLVNNKGLLHSDQQLFSGGSTNSQVKTYSTDPFTFYADFANAMIKMGKLSPLTGTDGQIRTDC | ||||||
Disulfide bond | 146↔171 | |||||
Sequence: CLMFRGRLYNETNIDSALATSLKSDC |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-264 | Plant heme peroxidase family profile | ||||
Sequence: MGASLLRMHFHDCFVNGCDASVLLDDISPSFTGEKTAGPNANSLRGFDVIDTIKSQVESICPGVVSCADILAVAARDSVVALGGPSWQVELGRRDSTTASYDAANTDLPSPLMDLSDLISALSRKGFTAKEMVALAGSHTIGQARCLMFRGRLYNETNIDSALATSLKSDCPTTGSDDNLSPLDATSPVIFDNSYFKNLVNNKGLLHSDQQLFSGGSTNSQVKTYSTDPFTFYADFANAMIKMGKLSPLTGTDGQIRTDCRKVN |
Sequence similarities
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length264
- Mass (Da)28,158
- Last updated2009-03-24 v1
- Checksum69514F899DBA44FD
Keywords
- Technical term