| IED ID | IndEnz0007000347 |
| Enzyme Type ID | catalase000347 |
| Protein Name |
Catalase-peroxidase 2 CP 2 EC 1.11.1.21 Peroxidase/catalase 2 |
| Gene Name | katG2 katP L7017 ECO57PM75 |
| Organism | Escherichia coli O157:H7 |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O157:H7 |
| Enzyme Sequence | MIKKTLPVLILLALSGSFSTAVAADKKETQNFYYPETLDLTPLRLHSPESNPWGADFDYATRFQQLDMEALKKDIKDLLTTSQDWWPADYGHYGPFFIRMAWHGAGTYRTYDGRGGASGGQQRFEPLNSWPDNVNLDKARRLLWPVKKKYGSSISWGDLMVLTGNVALESMGFKTLGFAGGREDDWESDLVYWGPDNKPLADNRDKNGKLQKPLAATQMGLIYVNPEGPGGKPDPLASAKDIREAFSRMAMDDEETVALIAGGHTFGKAHGAASPEKCIGAGPDGAPVEEQGLGWKNKCGTGNGKYTITSGLEGAWSTSPTQFTMQYLKNLYKYEWELHKSPAGAYQWKPKKAANIVQDAHDPSVLHPLMMFTTDIALKVDPEYKKITTRFLNDPKAFEQAFARAWFKLTHRDMGPAARYLGNEVPAESFIWQDPLPAADYTMIDGKDIKSLKEQVMDLGIPASELIKTAWASASTFRVTDYRGGNNGARIRLQPEINWEVNEPEKLKKVLASLTSLQREFNKKQSDGKKVSLADLIVLSGNAAIEDAARKAGVELEIPFTPGRTDASQEQTDVASFSVLEPTADGFRNYYSKSRSHISPVESLIDKASQLDLTVPEMTALLGGLRVMDINTNNSSLGVFTDTPGVLDNKFFVNLLDMSTRWSKADKEDTYNGFDRKTGALKWKASSVDLIFSSNPELRAVAEVYASDDARNKFIHDFVKSWNKVMNSDRFDLNNK |
| Enzyme Length | 736 |
| Uniprot Accession Number | Q7BSW8 |
| Absorption | |
| Active Site | ACT_SITE 103; /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. {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:8969527}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Cross-link (2); Metal binding (1); Signal peptide (1); Site (1) |
| Keywords | Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Periplasm;Peroxidase;Plasmid;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8969527}. |
| 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 | SIGNAL 1..23; /evidence=ECO:0000255|HAMAP-Rule:MF_01961 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Plasmid pO157 |
| Mass | 81,794 |
| Kinetics | |
| Metal Binding | METAL 264; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_01961 |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda |