Reviewed,
UniProtKB/Swiss-Prot P22196 (PER2_ARAHY)
Last modified
June 16, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Cationic peroxidase 2 EC=1.11.1.7 Alternative name(s): PNPC2 | ||
| Gene names |
| ||
| Organism | Arachis hypogaea (Peanut) | ||
| Taxonomic identifier | 3818 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Dalbergieae › Arachis |
Protein attributes
| Sequence length | 330 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| 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 | Donor + H2O2 = oxidized donor + 2 H2O. |
| Cofactor | Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro peroxidase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||||
| Chain | 24 – 330 | 307 | Cationic peroxidase 2 | PRO_0000023747 | |||||||
Sites | |||||||||||
| Active site | 72 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 73 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 76 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 78 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 80 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 82 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 194 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Metal binding | 195 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 246 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 249 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 254 | 1 | Calcium 2 By similarity | ||||||||
| Binding site | 164 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||||
| Site | 68 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 212 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 41 ↔ 117 | By similarity | |||||||||
| Disulfide bond | 74 ↔ 79 | By similarity | |||||||||
| Disulfide bond | 123 ↔ 326 | By similarity | |||||||||
| Disulfide bond | 201 ↔ 233 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells." Buffard D., Breda C., van Huystee R.B., Asemota O., Pierre M., Dang Ha D.B., Esnault R. Proc. Natl. Acad. Sci. U.S.A. 87:8874-8878(1990) [PubMed: 2247460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| M37637 mRNA. Translation: AAA32676.1. | |
| PIR | B38265. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PA2 based on UniProtKB Q42578. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 103. AhPrx05. |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.7. 569. |
Family and domain databases | |
| InterPro | IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| Pfam | PF00141. peroxidase. 1 hit. [Graphical view] |
| PRINTS | PR00458. PEROXIDASE. PR00461. PLPEROXIDASE. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PER2_ARAHY | ||||||||
| Accession | Primary (citable) accession number: P22196 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


