IED ID | IndEnz0007000499 |
Enzyme Type ID | catalase000499 |
Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Peroxidase/catalase |
Gene Name | katG An01g01830 |
Organism | Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
Enzyme Sequence | MAEAKCPFSQSRSNANVAGGGTRNTDWWPDQLNLGILRQHAPASNPFERDFDYTAAFNSLDYYALKKDLHALMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRVFDGRGGGGQGQQRFAPLNSWPDNASLDKARRLLWPIKQKYGAKISWADLMLLAGNVALESMGFKTYGFSGGRADTWEADESVYWGGESTWMGNDVRYSDGFPGVTKHGALSGDEPPHRNIHTRDLEKPLAASHMGLIYVNPEGPDGNPDPVAAARDIRTTFGRMGMNDEETVALIAGGHSFGKTHGAASSENVDVEPAAAGLENQGLGWSNRYQSGKGPHTITSGIEVTWTKTPTKWSHAFLEYLFRFDWELTKSPGGANQWQAKNTEAIIPDAYDPSKKHLPKMLTTDLSLRYDPAYEKIARRFLDHPDEFADAFSRAWFKLLHRDMGPRTRYIGPEAPTEDLIWQDPIPAVNHTLVDANDIAALKRTILDTGLNKSNFVSTAWASASTFRGTDKRGGANGARIRLAPQRQWEVNNQPWLEETLSALEKIQKDFNDRVSSTGKKISLADLIVLAGCAAVEKAAQEAGQTITVPFTPGRMDASQEQTEVESFSHLEPVADGFRNYGKSSSRVRAEHYLVDKAHLLTLTAPEMTVLVGGLRVLNTNYDGSKHGVLTSSPGRLTNDFFTNVLDMNTAWKAKDGGRDLYEGTDRKTGQPKWTATRADLVFGSHAELRALAEVYGSSDGQEKFVKDFVSAWDKVMNLDRFDLKGSGIARSKL |
Enzyme Length | 762 |
Uniprot Accession Number | A2Q7T1 |
Absorption | |
Active Site | ACT_SITE 97; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
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_03108}; 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_03108}; |
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_03108}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (1); Cross-link (2); Metal binding (1); Region (1); Site (1) |
Keywords | Cytoplasm;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}. |
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_03108}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 84,251 |
Kinetics | |
Metal Binding | METAL 283; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
Rhea ID | RHEA:30275; RHEA:20309 |
Cross Reference Brenda |