IED ID | IndEnz0018001074 |
Enzyme Type ID | peroxidase001074 |
Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Catalase-2 Peroxidase/catalase |
Gene Name | katG CAT2 AFUA_8G01670 |
Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Enzyme Sequence | MTQDKCPFKEQSSQPNFAGGGTSNKDWWPDRLKLNILRQHTAVSNPLDADFDYAAAFNSLDYEGLKKDLRALMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRVFDGRGGAGQGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGNKISWADLLILTGNVALESMGFKTFGFAGGRPDTWEADEATYWGRETTWLGNDARYAKGFSGSDKRGSLIADEESHKTTHSRELETPLAAAHMGLIYVNPEGPDGNPDPVAAAHDIRDTFGRMAMNDEETVALIAGGHTFGKTHGAAPADNVGKEPEAAGLEAQGLGWANKHGSGKGPHTITSGLEVTWTKTPTQWNNNFLEYLFKFEWELTKSPAGAHQWVAKNADEIIPDAYDASKKHKPTMLTTDLSLRFDPAYEKIARRFLEHPDQFADAFARAWFKLTHRDMGPRARYLGPEVPSEVLIWQDPIPAVNHPLVDASDIAALKDEILASGVPPRSFISTAWAAASTFRGSDKRGGANGARIRLAPQRDWEVNNQPWLREALSALEAVQSRFNARGDSKKVSLADLIVLAGCAAVEKAAQDAGHPIKVPFVPGRMDASQEETDVQSFNHMEPFADGFRNFAKGPARPRAEHYLVDKAQLLNLSAPEMTVLVGGLRVLNTNYDGSTHGVFTSRPGALTNDFFVHLLDMNTAWKDVGNGELFEGSDRKTGGKKWTATRADLVFGSNAELRAIAEVYASNDGDMKFVKDFVAAWNKVMNLDRFDLKGKQTIPARL |
Enzyme Length | 759 |
Uniprot Accession Number | Q7Z7W6 |
Absorption | |
Active Site | ACT_SITE 97; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
Activity Regulation | ACTIVITY REGULATION: Sensitive to heat and heavy metals. {ECO:0000269|PubMed:12761140}. |
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. May be involved in protection from the host during host infection. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:12761140}. |
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;Direct protein sequencing;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: Not glycosylated.; 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 | 83,762 |
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 |