| IED ID | IndEnz0018000730 |
| Enzyme Type ID | peroxidase000730 |
| Protein Name |
Peroxidase C1A EC 1.11.1.7 |
| Gene Name | PRXC1A HPRC1 |
| Organism | Armoracia rusticana (Horseradish) (Armoracia laphatifolia) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Cardamineae Armoracia Armoracia rusticana (Horseradish) (Armoracia laphatifolia) |
| Enzyme Sequence | MHFSSSSTLFTCITLIPLVCLILHASLSDAQLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNRSSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQKGLIQSDQELFSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVNSNSLLHDMVEVVDFVSSM |
| Enzyme Length | 353 |
| Uniprot Accession Number | P00433 |
| Absorption | |
| Active Site | ACT_SITE 72; /note=Proton acceptor |
| Activity Regulation | |
| Binding Site | BINDING 169; /note=Substrate; via carbonyl oxygen |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; |
| DNA Binding | |
| EC Number | 1.11.1.7 |
| Enzyme Function | 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (7); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (8); Helix (18); Metal binding (11); Modified residue (1); Propeptide (1); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Secreted;Signal;Vacuole |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles. |
| Modified Residue | MOD_RES 31; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:1001465" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000269|PubMed:1001465 |
| Structure 3D | X-ray crystallography (31) |
| Cross Reference PDB | 1ATJ; 1GW2; 1GWO; 1GWT; 1GWU; 1GX2; 1H55; 1H57; 1H58; 1H5A; 1H5C; 1H5D; 1H5E; 1H5F; 1H5G; 1H5H; 1H5I; 1H5J; 1H5K; 1H5L; 1H5M; 1HCH; 1KZM; 1W4W; 1W4Y; 2ATJ; 2YLJ; 3ATJ; 4ATJ; 6ATJ; 7ATJ; |
| Mapped Pubmed ID | 10574977; 12024218; 12351824; 15299344; 15641789; 2198290; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,825 |
| Kinetics | |
| Metal Binding | METAL 73; /note=Calcium 1; METAL 76; /note=Calcium 1; via carbonyl oxygen; METAL 78; /note=Calcium 1; via carbonyl oxygen; METAL 80; /note=Calcium 1; METAL 82; /note=Calcium 1; METAL 94; /note=Calcium 1; METAL 200; /note=Iron (heme b axial ligand); METAL 201; /note=Calcium 2; METAL 252; /note=Calcium 2; METAL 255; /note=Calcium 2; METAL 260; /note=Calcium 2 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda | 1.11.1.7; |