| IED ID | IndEnz0018001615 |
| Enzyme Type ID | peroxidase001615 |
| Protein Name |
Thiol peroxidase Tpx EC 1.11.1.24 Peroxiredoxin tpx Prx Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin Fragment |
| Gene Name | tpx |
| Organism | Streptococcus pneumoniae |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae |
| Enzyme Sequence | MTTFLGNPVTFTGSQLQVGDTAHDFSLTTPNLEKKSLADFAGKKKVLSVI |
| Enzyme Length | 50 |
| Uniprot Accession Number | P42365 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| 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:0000269|PubMed:9141476}; |
| 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:0000269|PubMed:9141476}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Initiator methionine (1); Non-terminal residue (1) |
| Keywords | Antioxidant;Direct protein sequencing;Oxidoreductase;Peroxidase;Redox-active center |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 5,355 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |