IED ID | IndEnz0018001255 |
Enzyme Type ID | peroxidase001255 |
Protein Name |
Catalase-peroxidase 2 CP 2 EC 1.11.1.21 Peroxidase/catalase 2 |
Gene Name | katG2 katA BceJ2315_55450 BCAM2107 |
Organism | Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Burkholderia Burkholderia cepacia complex Burkholderia cenocepacia Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)) |
Enzyme Sequence | MSNEGQCPFNHANGGGTTNRDWWPNELRLDLLSQHSSKTDPLDPGFNYAEAFNSLDLDALRKDLAALMTDSQDWWPADFGHYGPLFVRMAWHSAGTYRMGDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLLILTGDVALTTMGFKTFGYAGGREDTWEPDRDVYWGSETTWLGGDLRYDKGGACESQHGGNAGRNLENPLAAVQMGLIYVNPEGPDGNPDPVAAAYDIREVFGRMAMNDEETVALIAGGHAFGKTHGAGPADNVGLEPEAAGLEQQGLGWKNSFGTGKGADTITSGLEVTWSDTPTQWGMGFFKNLFGYEWELTKSPAGAHQWVAKNAEPTIPHAHDPSKKLLPTMLTTDLSLRFDPVYEKISRHFMDNPDVFADAFARAWFKLTHRDMGPRARYLGPDVPTEELIWQDPIPAVDHVLVDDTDVAPLKETILASGLSVAELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWAVNEPARLAKVLKVLERIQGEFNSTQPGGKKISLADLIVLAGGAGIEQAAKRAGHDVVVPFAPGRMDASQEQTDAHSFAVLEPVADGFRNFVKGKFAVPAEALLIDKAQLLTLTAPQMTALVGGLRVLNVQTGDEKHGVFTDQPETLTVDFFRNLLDMATEWKPIAGEDTYEGRDRRTGELKWTGTRVDLVFGSNAVLRALSEVYASADGEAKFIRDFVAAWVKVMNLDRFDLA |
Enzyme Length | 736 |
Uniprot Accession Number | Q4F6N6 |
Absorption | |
Active Site | ACT_SITE 92; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01961 |
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. Shows peroxidase specificity towards odianisidine, ABTS and pyrogallol, but methoxyphenol and 2-chloronaphthol are not peroxidized. {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:17371508}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 for the peroxidase reaction and 6.0 for the catalase reaction. Active from pH 5.5 to 8.5. {ECO:0000269|PubMed:17371508}; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Cross-link (2); Metal binding (1); Site (1) |
Keywords | 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 | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 80,487 |
Kinetics | |
Metal Binding | METAL 268; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_01961 |
Rhea ID | RHEA:30275; RHEA:20309 |
Cross Reference Brenda | 1.11.1.6; |