| IED ID | IndEnz0018001407 | 
| Enzyme Type ID | peroxidase001407 | 
| Protein Name | 
                        
                            
                                Vanadium chloroperoxidase  EC 1.11.1.10 Vanadium chloride peroxidase VCPO  | 
                    
| Gene Name | CPO | 
| Organism | Curvularia inaequalis | 
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Pleosporaceae Curvularia Curvularia inaequalis | 
| Enzyme Sequence | MGSVTPIPLPKIDEPEEYNTNYILFWNHVGLELNRVTHTVGGPLTGPPLSARALGMLHLAIHDAYFSICPPTDFTTFLSPDTENAAYRLPSPNGANDARQAVAGAALKMLSSLYMKPVEQPNPNPGANISDNAYAQLGLVLDRSVLEAPGGVDRESASFMFGEDVADVFFALLNDPRGASQEGYHPTPGRYKFDDEPTHPVVLIPVDPNNPNGPKMPFRQYHAPFYGKTTKRFATQSEHFLADPPGLRSNADETAEYDDAVRVAIAMGGAQALNSTKRSPWQTAQGLYWAYDGSNLIGTPPRFYNQIVRRIAVTYKKEEDLANSEVNNADFARLFALVDVACTDAGIFSWKEKWEFEFWRPLSGVRDDGRPDHGDPFWLTLGAPATNTNDIPFKPPFPAYPSGHATFGGAVFQMVRRYYNGRVGTWKDDEPDNIAIDMMISEELNGVNRDLRQPYDPTAPIEDQPGIVRTRIVRHFDSAWELMFENAISRIFLGVHWRFDAAAARDILIPTTTKDVYAVDNNGATVFQNVEDIRYTTRGTREDPEGLFPIGGVPLGIEIADEIFNNGLKPTPPEIQPMPQETPVQKPVGQQPVKGMWEEEQAPVVKEAP | 
| Enzyme Length | 609 | 
| Uniprot Accession Number | P49053 | 
| Absorption | |
| Active Site | ACT_SITE 404 | 
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.; EC=1.11.1.10; | 
| DNA Binding | |
| EC Number | 1.11.1.10 | 
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (14); Chain (1); Helix (22); Metal binding (1); Region (1); Sequence conflict (1); Turn (5) | 
| Keywords | 3D-structure;Chloride;Direct protein sequencing;Metal-binding;Oxidoreductase;Peroxidase;Secreted;Vanadium | 
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. | 
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. | 
| Signal Peptide | |
| Structure 3D | X-ray crystallography (10) | 
| Cross Reference PDB | 1IDQ; 1IDU; 1VNC; 1VNE; 1VNF; 1VNG; 1VNH; 1VNI; 1VNS; 3BB0; | 
| Mapped Pubmed ID | 10499093; 18163651; 9165086; | 
| Motif | |
| Gene Encoded By | |
| Mass | 67,531 | 
| Kinetics | |
| Metal Binding | METAL 496; /note=Vanadium | 
| Rhea ID | |
| Cross Reference Brenda | 1.11.1.B2; |