A0A8T9EH72 · A0A8T9EH72_9ROSI
- ProteinPeroxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids306 (go to sequence)
- Protein existenceEvidence at transcript level
- 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 | 43 | Transition state stabilizer | |||
Active site | 47 | Proton acceptor | |||
Binding site | 48 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 51 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 53 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 55 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 57 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 139 | substrate | |||
Binding site | 169 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 170 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 222 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 230 | Ca2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plant-type cell wall | |
Cellular Component | plasmodesma | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | peroxidase activity | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxidase
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Malpighiales > Euphorbiaceae > Crotonoideae > Aleuritideae > Vernicia
Accessions
- Primary accessionA0A8T9EH72
Subcellular Location
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Disulfide bond | 16↔92 | ||||
Disulfide bond | 49↔54 | ||||
Disulfide bond | 98↔302 | ||||
Disulfide bond | 176↔209 | ||||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 6-306 | Plant heme peroxidase family profile | |||
Sequence similarities
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Family and domain databases
Sequence
- Sequence statusFragment
- Length306
- Mass (Da)32,909
- Last updated2022-10-12 v1
- MD5 ChecksumE05A7F5BE0CDB1460D7C647F1E01A98B
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MW051683 EMBL· GenBank· DDBJ | UNA06901.1 EMBL· GenBank· DDBJ | mRNA |