Reviewed,
UniProtKB/Swiss-Prot P85347 (PER2_CYCRE)
Last modified
June 16, 2009.
Version 8.
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: Peroxidase 2 EC=1.11.1.7 |
| Organism | Cycas revoluta (Sago palm) |
| Taxonomic identifier | 3396 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Cycadophyta › Cycadales › Cycadaceae › Cycas |
Protein attributes
| Sequence length | 15 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein 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. UniProtKB P22195 |
| Cofactor | Binds 2 calcium ions per subunit By similarity. UniProtKB P22195 Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. UniProtKB P22195 |
| Subcellular location | Secreted By similarity. UniProtKB P84516 |
| Sequence similarities | Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Cellular component | Secreted |
| Ligand | Calcium Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Direct protein sequencing |
| 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 iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›15 | ›15 | Peroxidase 2 | PRO_0000315884 | |||||
Sites | |||||||||
| Metal binding | 9 | 1 | Iron (heme axial ligand) By similarity UniProtKB P22195 | ||||||
| Metal binding | 10 | 1 | Calcium 2 By similarity UniProtKB P22195 | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 15 | 1 | |||||||
Sequences
References
| [1] | Novo Uzal E., Gomez Ros L.V., Ros Barcelo A. Submitted (NOV-2007) to UniProtKB Cited for: PROTEIN SEQUENCE. Tissue: Callus. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.7. 264682. |
Family and domain databases | |
| InterPro | IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. Partial match. PS50873. PEROXIDASE_4. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PER2_CYCRE | ||||||||
| Accession | Primary (citable) accession number: P85347 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


