| IED ID | IndEnz0007000009 |
| Enzyme Type ID | catalase000009 |
| Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Peroxidase/catalase |
| Gene Name | katG Synpcc7942_1656 |
| Organism | Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Synechococcaceae Synechococcus Synechococcus elongatus Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2) |
| Enzyme Sequence | MTATQGKCPVMHGGATTVNISTAEWWPKALNLDILSQHDRKTNPMGPDFNYQEEVKKLDVAALKQDLQALMTDSQDWWPADWGHYGGLMIRLTWHAAGTYRIADGRGGAGTGNQRFAPLNSWPDNTNLDKARRLLWPIKQKYGNKLSWADLIAYAGTIAYESMGLKTFGFAFGREDIWHPEKDIYWGPEKEWVPPSTNPNSRYTGDRELENPLAAVTMGLIYVNPEGVDGNPDPLKTAHDVRVTFARMAMNDEETVALTAGGHTVGKCHGNGNAALLGPEPEGADVEDQGLGWINKTQSGIGRNAVTSGLEGAWTPHPTQWDNGYFRMLLNYDWELKKSPAGAWQWEPINPREEDLPVDVEDPSIRRNLVMTDADMAMKMDPEYRKISERFYQDPAYFADVFARAWFKLTHRDMGPKARYIGPDVPQEDLIWQDPIPAGNRNYDVQAVKDRIAASGLSISELVSTAWDSARTYRNSDKRGGANGARIRLAPQKDWEGNEPDRLAKVLAVLEGIAAATGASVADVIVLAGNVGVEQAARAAGVEIVLPFAPGRGDATAEQTDTESFAVLEPIHDGYRNWLKQDYAATPEELLLDRTQLLGLTAPEMTVLIGGLRVLGTNHGGTKHGVFTDREGVLTNDFFVNLTDMNYLWKPAGKNLYEICDRKTNQVKWTATRVDLVFGSNSILRAYSELYAQDDNKEKFVRDFVAAWTKVMNADRFDLD |
| Enzyme Length | 720 |
| Uniprot Accession Number | Q31MN3 |
| Absorption | |
| Active Site | ACT_SITE 95; /note=Proton acceptor |
| Activity Regulation | |
| 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. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for catalase activity. Active from pH 4.5 to 8.5. {ECO:0000269|PubMed:8645214}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (16); Chain (1); Cross-link (2); Frameshift (1); Helix (46); Initiator methionine (1); Metal binding (1); Sequence conflict (10); Site (1); Turn (7) |
| Keywords | 3D-structure;Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| 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 | X-ray crystallography (5) |
| Cross Reference PDB | 1UB2; 3WNU; 3WXO; 3X16; 4PAE; |
| Mapped Pubmed ID | 24598912; 25303560; 25479089; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,078 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.2 mM for H(2)O(2) for catalase activity {ECO:0000269|PubMed:8645214}; |
| Metal Binding | METAL 263; /note=Iron (heme b axial ligand) |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda | 1.11.1.21; |