| IED ID | IndEnz0007000343 |
| Enzyme Type ID | catalase000343 |
| Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Peroxidase/catalase |
| Gene Name | katG syc2431_d |
| Organism | Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Synechococcaceae Synechococcus Synechococcus elongatus Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) |
| Enzyme Sequence | MTATQGKCPVMHGGATTVNISTAEWWPKALNLDILSQHDRKTNPMGPDFNYQEEVKKLDVAALKQDLQALMTDSQDWWPADWGHYGGLMIRLTWHAAGTYRIADGRGGAGTGNQRFAPLNSWPDNTNLDKARRLLWPIKQKYGNKLSWADLIAYAGTIAYESMGLKTFGFAFGREDIWHPEKDIYWGPEKEWVPPSTNPNSRYTGDRELENPLAAVTMGLIYVNPEGVDGNPDPLKTAHDVRVTFARMAMNDEETVALTAGGHTVGKCHGNGNAALLGPEPEGADVEDQGLGWINKTQSGIGRNAVTSGLEGAWTPHPTQWDNGYFRMLLNYDWELKKSPAGAWQWEPINPREEDLPVDVEDPSIRRNLVMTDADMAMKMDPEYRKISERFYQDPAYFADVFARAWFKLTHRDMGPKARYIGPDVPQEDLIWQDPIPAGNRNYDVQAVKDRIAASGLSISELVSTAWDSARTYRNSDKRGGANGARIRLAPQKDWEGNEPDRLAKVLAVLEGIAAATGASVADVIVLAGNVGVEQAARAAGVEIVLPFAPGRGDATAEQTDTESFAVLEPIHDGYRNWLKQDYAATPEELLLDRTQLLGLTAPEMTVLIGGLRVLGTNHGGTKHGVFTDREGVLTNDFFVNLTDMNYLWKPAGKNLYEICDRKTNQVKWTATRVDLVFGSNSILRAYSELYAQDDNKEKFVRDFVAAWTKVMNADRFDLD |
| Enzyme Length | 720 |
| Uniprot Accession Number | Q5MZ99 |
| Absorption | |
| Active Site | ACT_SITE 95; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01961 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by cyanide. {ECO:0000269|PubMed:10863004}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; |
| DNA Binding | |
| EC Number | 1.11.1.21 |
| Enzyme Function | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:10863004, ECO:0000269|PubMed:9207193}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5 for both the catalase and the peroxidase reaction. {ECO:0000269|PubMed:9207193}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Cross-link (2); Metal binding (1); Sequence conflict (2); Site (1) |
| Keywords | Cytoplasm;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9207193}. |
| Modified Residue | |
| Post Translational Modification | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,078 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 mM for H(2)O(2) for the catalase reaction {ECO:0000269|PubMed:9207193}; |
| Metal Binding | METAL 263; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_01961 |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda |