| IED ID | IndEnz0018001654 |
| Enzyme Type ID | peroxidase001654 |
| Protein Name |
Peroxiredoxin EC 1.11.1.24 Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin |
| Gene Name | ahpC PH1217 |
| Organism | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus horikoshii Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Enzyme Sequence | MVVIGEKFPEVEVKTTHGVIKLPDYFTKQGKWFILFSHPADFTPVCTTEFYGMQKRVEEFRKLGVEPIGLSVDQVFSHIKWIEWIKDNLSVEIDFPVIADDRGELAEKLGMIPSGATITARAVFVVDDKGIIRAIVYYPAEVGRDWDEILRLVKALKISTEKGVALPHKWPNNELIGDKVIVPPASTIEEKKQREEAKAKGEIECYDWWFCYKKLE |
| Enzyme Length | 216 |
| Uniprot Accession Number | O58966 |
| Absorption | |
| Active Site | ACT_SITE 46; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:23832195" |
| Activity Regulation | |
| Binding Site | BINDING 121; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00401 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12944367, ECO:0000269|PubMed:15625325}; |
| DNA Binding | |
| EC Number | 1.11.1.24 |
| Enzyme Function | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12944367, ECO:0000269|PubMed:15625325}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Retains full activity after 20 minutes at 90 degrees Celsius and 75 % of its initial activity after 20 minutes at 100 degrees Celsius. {ECO:0000269|PubMed:15625325}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.8. {ECO:0000269|PubMed:15625325}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Binding site (1); Chain (1); Disulfide bond (3); Domain (1); Helix (8); Initiator methionine (1); Turn (3) |
| Keywords | 3D-structure;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center |
| Interact With | |
| Induction | INDUCTION: Up-regulated by exposure to oxygen (at protein level). {ECO:0000269|PubMed:12944367, ECO:0000269|PubMed:15625325}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3W6G; 5XBQ; 5XBR; 6IU1; |
| Mapped Pubmed ID | 28992240; 30796432; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,757 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |