IED ID | IndEnz0018000743 |
Enzyme Type ID | peroxidase000743 |
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; |