Q96511 · PER69_ARATH
- ProteinPeroxidase 69
- GenePER69
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids331 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Miscellaneous
There are 73 peroxidase genes in A.thaliana.
Catalytic activity
- 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Note: Binds 2 calcium ions per subunit.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 73 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 77 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 78 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 81 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 83 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 85 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 87 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 168 | substrate | ||||
Sequence: P | ||||||
Binding site | 198 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 199 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 248 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 251 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 256 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Cellular Component | plasmodesma | |
Molecular Function | heme binding | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA 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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxidase 69
- EC number
- Short namesAtperox P69
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ96511
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MGRGYNLLFVLVTFLVLVAAVTA | ||||||
Chain | PRO_0000023734 | 24-331 | Peroxidase 69 | |||
Sequence: QGNRGSNSGGGRRPHVGFYGNRCRNVESIVRSVVQSHVRSIPANAPGILRMHFHDCFVHGCDGSVLLAGNTSERTAVPNRSLRGFEVIEEAKARLEKACPRTVSCADILTLAARDAVVLTGGQRWEVPLGRLDGRISQASDVNLPGPSDSVAKQKQDFAAKTLNTLDLVTLVGGHTIGTAGCGLVRGRFVNFNGTGQPDPSIDPSFVPLILAQCPQNGGTRVELDEGSVDKFDTSFLRKVTSSRVVLQSDLVLWKDPETRAIIERLLGLRRPSLRFGTEFGKSMVKMSLIEVKTGSDGEIRRVCSAIN | ||||||
Disulfide bond | 46↔122 | |||||
Sequence: CRNVESIVRSVVQSHVRSIPANAPGILRMHFHDCFVHGCDGSVLLAGNTSERTAVPNRSLRGFEVIEEAKARLEKAC | ||||||
Disulfide bond | 79↔84 | |||||
Sequence: CFVHGC | ||||||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 128↔327 | |||||
Sequence: CADILTLAARDAVVLTGGQRWEVPLGRLDGRISQASDVNLPGPSDSVAKQKQDFAAKTLNTLDLVTLVGGHTIGTAGCGLVRGRFVNFNGTGQPDPSIDPSFVPLILAQCPQNGGTRVELDEGSVDKFDTSFLRKVTSSRVVLQSDLVLWKDPETRAIIERLLGLRRPSLRFGTEFGKSMVKMSLIEVKTGSDGEIRRVC | ||||||
Disulfide bond | 205↔237 | |||||
Sequence: CGLVRGRFVNFNGTGQPDPSIDPSFVPLILAQC | ||||||
Glycosylation | 216 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Mainly expressed in roots and slightly in leaves.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length331
- Mass (Da)35,679
- Last updated1997-02-01 v1
- Checksum4906CDF9648BD060
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X98808 EMBL· GenBank· DDBJ | CAA67340.1 EMBL· GenBank· DDBJ | mRNA | ||
AB008266 EMBL· GenBank· DDBJ | BAB10278.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED97840.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY093012 EMBL· GenBank· DDBJ | AAM13011.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |