| IED ID | IndEnz0018001482 |
| Enzyme Type ID | peroxidase001482 |
| Protein Name |
Peroxiredoxin bcp1 Prx EC 1.11.1.24 Bacterioferritin comigratory protein 1 BCP Nuclear thiol peroxidase nTPx Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin bcp1 |
| Gene Name | bcp1 SPBC1773.02c |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MDAPRRSSRLAAKIANVLDSKGTIIPEAAPVMLKKPAKDESVDSTIQVGDVIPDITLPDEDGTSIRLRDITANKGLVIFAYPKASTPGCTKQGCGFRDNYPKIQASDYEVLGLSFDTSKAQKAFKDKQNFPYHLLSDPKGELIKKLGAEKPGGGKLFRSHWIFEKGTGKCIVKEIDISPLVSVDKAFAVITDSEP |
| Enzyme Length | 195 |
| Uniprot Accession Number | O94561 |
| Absorption | |
| Active Site | ACT_SITE 89; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P40553 |
| 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:0000250|UniProtKB:P40553}; |
| 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 and as sensor of hydrogen peroxide-mediated signaling events (By similarity). Acts as a scavenger of H(2)O(2) (PubMed:20356456). {ECO:0000250|UniProtKB:P40553, ECO:0000269|PubMed:20356456}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1) |
| Keywords | Antioxidant;Cytoplasm;Disulfide bond;Nucleus;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. |
| Modified Residue | |
| Post Translational Modification | PTM: The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin. {ECO:0000250|UniProtKB:P40553}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 23697806; 24521463; 25452419; 26537787; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,164 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |