Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
| PPepDB ID | PPepDB_4490 |
| Peptide Name | PER1A_ARMRU |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Armoracia rusticana, Armoracia laphatifolia |
| Plant Source (Common Name) | Horseradish |
| Plant Family | Brassicaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole | Peroxidase C1A precursor (EC 1.11.1.7).Secreted (Probable). Vacuole (Probable). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | ANSARGFPVIDRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPFDLRTPTIFDNKYYVNLEEQKGLIQSDQELFSSPNATDTIPLVRSFANSTLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNRSSDLVALSGGHMHFSSSSTLFTCITLIPLVCLILHASLSDAQLTPTFYDNSCPNVSNIVRDQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVNSNSLLHDMVEVVDFVSSMTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGN |
| Sequence Length | 353 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 38825.09 |
| Monoisotopic Molecular Weight (Da) | 38800.41 |
| Isoelectric Point (pI) | 5.68 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
| Uniprot | P00433 |
| NCBI | --NA-- |
| EMBL | M37156 |
| Link to Source Databases | SPdb187718 |
| Addtional Information | FUNCTION:Removal of H(2)O(2), 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 H(2)O(2) = oxidized donor 2 H(2)O.COFACTOR:Binds 2 calcium ions per subunit.COFACTOR:Binds 1 heme B (iron-protoporphyrin IX) group per subunit.SUBUNIT:Monomer.Note=Carboxy-terminal extension appears to target the protein to vacuoles.SIMILARITY:Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily. |