O80912 · PER23_ARATH
- ProteinPeroxidase 23
- GenePER23
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids349 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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 | 67 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 71 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 72 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 75 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 77 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 79 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 81 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 168 | substrate | ||||
Sequence: P | ||||||
Binding site | 199 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 200 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 251 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 254 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 259 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | vacuole | |
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 23
- EC number
- Short namesAtperox P23
- 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 accessionO80912
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for signal, modified residue, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MGFSSSLSCSAMGALIVGCLLLQASNSNA | ||||||
Modified residue | 30 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000023689 | 30-349 | Peroxidase 23 | |||
Sequence: QLRPDFYFRTCPPIFNIIGDTIVNELRTDPRIAASLLRLHFHDCFVRGCDASILLDNSTSFRTEKDAAPNKNSVRGFDVIDRMKAAIERACPRTVSCADIITIASQISVLLSGGPWWPVPLGRRDSVEAFFALANTALPSPFSTLTQLKTAFADVGLNRPSDLVALSGGHTFGKAQCQFVTPRLYNFNGTNRPDPSLNPTYLVELRRLCPQNGNGTVLVNFDSVTPTTFDRQYYTNLLNGKGLIQSDQVLFSTPGADTIPLVNQYSSNTFVFFGAFVDAMIRMGNLKPLTGTQGEIRQNCRVVNPRIRVVENDDGVVSSI | ||||||
Disulfide bond | 40↔120 | |||||
Sequence: CPPIFNIIGDTIVNELRTDPRIAASLLRLHFHDCFVRGCDASILLDNSTSFRTEKDAAPNKNSVRGFDVIDRMKAAIERAC | ||||||
Disulfide bond | 73↔78 | |||||
Sequence: CFVRGC | ||||||
Glycosylation | 86 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 126↔329 | |||||
Sequence: CADIITIASQISVLLSGGPWWPVPLGRRDSVEAFFALANTALPSPFSTLTQLKTAFADVGLNRPSDLVALSGGHTFGKAQCQFVTPRLYNFNGTNRPDPSLNPTYLVELRRLCPQNGNGTVLVNFDSVTPTTFDRQYYTNLLNGKGLIQSDQVLFSTPGADTIPLVNQYSSNTFVFFGAFVDAMIRMGNLKPLTGTQGEIRQNC | ||||||
Disulfide bond | 206↔238 | |||||
Sequence: CQFVTPRLYNFNGTNRPDPSLNPTYLVELRRLC | ||||||
Glycosylation | 217 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 243 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By methyl jasmonate, a plant defense-related signaling molecule.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length349
- Mass (Da)38,100
- Last updated1998-11-01 v1
- Checksum74A1C6F71A415169
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF452385 EMBL· GenBank· DDBJ | AAL40849.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004683 EMBL· GenBank· DDBJ | AAC28765.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC09531.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY099555 EMBL· GenBank· DDBJ | AAM20407.1 EMBL· GenBank· DDBJ | mRNA | ||
BT001238 EMBL· GenBank· DDBJ | AAN65125.1 EMBL· GenBank· DDBJ | mRNA |