| IED ID | IndEnz0018001643 | 
| Enzyme Type ID | peroxidase001643 | 
| Protein Name | 
                        
                            
                                Chloroperoxidase  EC 1.11.1.10 Chloride peroxidase CPO  | 
                    
| Gene Name | CPO | 
| Organism | Leptoxyphium fumago (Caldariomyces fumago) | 
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Dothideomycetidae Capnodiales Capnodiaceae Leptoxyphium Leptoxyphium fumago (Caldariomyces fumago) | 
| Enzyme Sequence | MFSKVLPFVGAVAALPHSVRQEPGSGIGYPYDNNTLPYVAPGPTDSRAPCPALNALANHGYIPHDGRAISRETLQNAFLNHMGIANSVIELALTNAFVVCEYVTGSDCGDSLVNLTLLAEPHAFEHDHSFSRKDYKQGVANSNDFIDNRNFDAETFQTSLDVVAGKTHFDYADMNEIRLQRESLSNELDFPGWFTESKPIQNVESGFIFALVSDFNLPDNDENPLVRIDWWKYWFTNESFPYHLGWHPPSPAREIEFVTSASSAVLAASVTSTPSSLPSGAIGPGAEAVPLSFASTMTPFLLATNAPYYAQDPTLGPNDKREAAPAATTSMAVFKNPYLEAIGTQDIKNQQAYVSSKAAAMASAMAANKARNL | 
| Enzyme Length | 373 | 
| Uniprot Accession Number | P04963 | 
| Absorption | |
| Active Site | ACT_SITE 204 | 
| 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 | FUNCTION: Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (4); Chain (1); Disulfide bond (1); Frameshift (2); Glycosylation (14); Helix (11); Metal binding (4); Modified residue (1); Mutagenesis (1); Propeptide (1); Signal peptide (1); Turn (6) | 
| Keywords | 3D-structure;Chloride;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Iron;Manganese;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Signal | 
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 21; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:8747463 | 
| Post Translational Modification | PTM: N- and O-glycosylated. | 
| Signal Peptide | SIGNAL 1..20 | 
| Structure 3D | X-ray crystallography (13) | 
| Cross Reference PDB | 1CPO; 2CIV; 2CIW; 2CIX; 2CIY; 2CIZ; 2CJ0; 2CJ1; 2CJ2; 2CPO; 2J18; 2J19; 2J5M; | 
| Mapped Pubmed ID | 16790441; 17190816; 17211068; | 
| Motif | |
| Gene Encoded By | |
| Mass | 40,504 | 
| Kinetics | |
| Metal Binding | METAL 50; /note=Iron (heme axial ligand); METAL 125; /note=Manganese; METAL 126; /note=Manganese; via carbonyl oxygen; METAL 129; /note=Manganese | 
| Rhea ID | |
| Cross Reference Brenda | 1.11.1.10; |