| IED ID | IndEnz0018000617 |
| Enzyme Type ID | peroxidase000617 |
| Protein Name |
Catalase-peroxidase 2 CP 2 EC 1.11.1.21 Peroxidase/catalase 2 |
| Gene Name | katG2 Hmcp rrnAC1171 |
| Organism | Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Halobacteriales Haloarculaceae Haloarcula Haloarcula marismortui Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) |
| Enzyme Sequence | MAETPNSDMSGATGGRSKRPKSNQDWWPSKLNLEILDQNARDVGPVEDDFDYAEEFQKLDLEAVKSDLEELMTSSQDWWPADYGHYGPLFIRMAWHSAGTYRTADGRGGAAGGRQRFAPINSWPDNANLDKARRLLLPIKQKYGQKISWADLMILAGNVAIESMGFKTFGYAGGREDAFEEDKAVNWGPEDEFETQERFDEPGEIQEGLGASVMGLIYVNPEGPDGNPDPEASAKNIRQTFDRMAMNDKETAALIAGGHTFGKVHGADDPEENLGPEPEAAPIEQQGLGWQNKNGNSKGGEMITSGIEGPWTQSPTEWDMGYINNLLDYEWEPEKGPGGAWQWAPKSEELKNSVPDAHDPDEKQTPMMLTTDIALKRDPDYREVMETFQENPMEFGMNFAKAWYKLTHRDMGPPERFLGPEVPDEEMIWQDPLPDADYDLIGDEEIAELKEEILDSDLSVSQLVKTAWASASTYRDSDKRGGANGARLRLEPQKNWEVNEPEQLETVLGTLENIQTEFNDSRSDGTQVSLADLIVLGGNAAVEQAAANAGYDVEIPFEPGRVDAGPEHTDAPSFDALKPKVDGVRNYIQDDITRPAEEVLVDNADLLNLTASELTALIGGMRSIGANYQDTDLGVFTDEPETLTNDFFVNLLDMGTEWEPAADSEHRYKGLDRDTGEVKWEATRIDLIFGSNDRLRAISEVYGSADAEKKLVHDFVDTWSKVMKLDRFDLE |
| Enzyme Length | 731 |
| Uniprot Accession Number | O59651 |
| Absorption | |
| Active Site | ACT_SITE 96; /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. {ECO:0000255|HAMAP-Rule:MF_01961}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (18); Chain (1); Cross-link (2); Erroneous initiation (1); Helix (45); Initiator methionine (1); Metal binding (1); Region (1); Site (1); Turn (9) |
| Keywords | 3D-structure;Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome |
| 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 (8) |
| Cross Reference PDB | 1ITK; 3UW8; 3VLH; 3VLI; 3VLJ; 3VLK; 3VLL; 3VLM; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 81,384 |
| Kinetics | |
| Metal Binding | METAL 259; /note=Iron (heme b axial ligand) |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda | 1.11.1.21; |