Q9SLH7 · PER20_ARATH
- ProteinPeroxidase 20
- GenePER20
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids336 (go to sequence)
- Protein existenceEvidence at transcript 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.
May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway.
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 | 66 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 70 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 71 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 74 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 76 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 78 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 80 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 167 | substrate | ||||
Sequence: P | ||||||
Binding site | 197 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 198 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 252 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 255 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 260 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
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
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxidase 20
- EC number
- Short namesAtperox P20
- 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 accessionQ9SLH7
- 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 | 1-24 | |||||
Sequence: MEIKQKKVWLSLIVLYAITTSVLG | ||||||
Chain | PRO_0000023686 | 25-336 | Peroxidase 20 | |||
Sequence: DFGEPLLKGFYKESCPLAEEIVKHNIEVAVLKDPRMAASLLRLQFHDCFVLGCDASVLLDTHGDMLSEKQATPNLNSLRGFEVIDYIKYLLEEACPLTVSCSDILALAARDSVFLRGGPWWEVLLGRRDSLKASFAGANQFIPAPNSSLDSLIINFKQQGLNIQDLIALSGAHTIGKARCVSFKQRIVQPNMEQTFYVDEFRRHSTFRRVLGSQCKDSSRDNELSPLDIKTPAYFDNHYFINLLEGRGLLISDNVLVSEDHEGEIFQKVWEYAVNQDLFFIDFVESMLKMGNINVLTGIEGEIRENCRFVNI | ||||||
Disulfide bond | 39↔119 | |||||
Sequence: CPLAEEIVKHNIEVAVLKDPRMAASLLRLQFHDCFVLGCDASVLLDTHGDMLSEKQATPNLNSLRGFEVIDYIKYLLEEAC | ||||||
Disulfide bond | 72↔77 | |||||
Sequence: CFVLGC | ||||||
Disulfide bond | 125↔331 | |||||
Sequence: CSDILALAARDSVFLRGGPWWEVLLGRRDSLKASFAGANQFIPAPNSSLDSLIINFKQQGLNIQDLIALSGAHTIGKARCVSFKQRIVQPNMEQTFYVDEFRRHSTFRRVLGSQCKDSSRDNELSPLDIKTPAYFDNHYFINLLEGRGLLISDNVLVSEDHEGEIFQKVWEYAVNQDLFFIDFVESMLKMGNINVLTGIEGEIRENC | ||||||
Glycosylation | 170 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 204↔239 | |||||
Sequence: CVSFKQRIVQPNMEQTFYVDEFRRHSTFRRVLGSQC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Late induced by benzothiadiazol, a chemical analog of salicylic acid. Enhanced expression following incompatible bacterial pathogen attack.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q9SLH7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length336
- Mass (Da)37,978
- Last updated2000-05-01 v1
- Checksum46AE9705043D3EC3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4IJW0 | F4IJW0_ARATH | At2g35380 | 248 |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC005314 EMBL· GenBank· DDBJ | AAC36183.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC09101.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117626 EMBL· GenBank· DDBJ | BAC42282.1 EMBL· GenBank· DDBJ | mRNA | ||
BT004975 EMBL· GenBank· DDBJ | AAO50508.1 EMBL· GenBank· DDBJ | mRNA | ||
Y11793 EMBL· GenBank· DDBJ | CAA72489.1 EMBL· GenBank· DDBJ | mRNA |