Detail Information for IndEnz0007000715
IED ID IndEnz0007000715
Enzyme Type ID catalase000715
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;