O23474 · PER40_ARATH
- ProteinPeroxidase 40
- GenePER40
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids348 (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 | 86 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 90 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 91 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 94 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 96 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 98 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 100 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 187 | substrate | ||||
Sequence: P | ||||||
Binding site | 217 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 218 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 269 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 272 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 277 | 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 40
- EC number
- Short namesAtperox P40
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO23474
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MKNLFNLFLMFFFAMPILSLS | ||||||
Chain | PRO_0000023706 | 22-348 | Peroxidase 40 | |||
Sequence: ENPTNFSESCEDGSGETGSSFGIGFDLVLDFGLYRNSCPEAESIVYSWVETTVLEDPRMAASLLRLHFHDCFVNGCDASVLLDDTEGLVGEKTAPPNLNSLRGFEVIDSIKSDIESVCPETVSCADILAMAARDSVVVSGGPRWEVEVGRKDSRTASKQAATNGLPSPNSTVSTLISTFQNLGLSQTDMVALSGGHTLGKARCTSFTARLQPLQTGQPANHGDNLEFLESLQQLCSTVGPSVGITQLDLVTPSTFDNQYYVNLLSGEGLLPSDQALAVQDPGTRAIVETYATDQSVFFEDFKNAMVKMGGIPGGSNSEIRKNCRMIN | ||||||
Glycosylation | 26 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 59↔139 | |||||
Sequence: CPEAESIVYSWVETTVLEDPRMAASLLRLHFHDCFVNGCDASVLLDDTEGLVGEKTAPPNLNSLRGFEVIDSIKSDIESVC | ||||||
Disulfide bond | 92↔97 | |||||
Sequence: CFVNGC | ||||||
Disulfide bond | 145↔344 | |||||
Sequence: CADILAMAARDSVVVSGGPRWEVEVGRKDSRTASKQAATNGLPSPNSTVSTLISTFQNLGLSQTDMVALSGGHTLGKARCTSFTARLQPLQTGQPANHGDNLEFLESLQQLCSTVGPSVGITQLDLVTPSTFDNQYYVNLLSGEGLLPSDQALAVQDPGTRAIVETYATDQSVFFEDFKNAMVKMGGIPGGSNSEIRKNC | ||||||
Glycosylation | 190 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 224↔256 | |||||
Sequence: CTSFTARLQPLQTGQPANHGDNLEFLESLQQLC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 170-189 | Disordered | ||||
Sequence: GRKDSRTASKQAATNGLPSP |
Sequence similarities
Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length348
- Mass (Da)37,460
- Last updated2002-12-06 v2
- Checksum1B438813818178E5
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z97340 EMBL· GenBank· DDBJ | CAB10406.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161543 EMBL· GenBank· DDBJ | CAB78669.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE83724.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT011747 EMBL· GenBank· DDBJ | AAS49110.1 EMBL· GenBank· DDBJ | mRNA | ||
AK175661 EMBL· GenBank· DDBJ | BAD43424.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK175982 EMBL· GenBank· DDBJ | BAD43745.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |