| IED ID | IndEnz0018000163 |
| Enzyme Type ID | peroxidase000163 |
| Protein Name |
Peroxiredoxin Bcp EC 1.11.1.24 Bacterioferritin comigratory protein Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin Bcp |
| Gene Name | bcp XCC1738 |
| Organism | Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xanthomonas Xanthomonas campestris Xanthomonas campestris pv. campestris Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) |
| Enzyme Sequence | MTDAVLELPAATFDLPLSLSGGTQTTLRAHAGHWLVIYFYPKDSTPGCTTEGLDFNALLPEFDKAGAKILGVSRDSVKSHDNFCAKQGFAFPLVSDGDEALCRAFDVIKEKNMYGKQVLGIERSTFLLSPEGQVVQAWRKVKVAGHADAVLAALKAHAKQ |
| Enzyme Length | 160 |
| Uniprot Accession Number | Q8P9V9 |
| Absorption | |
| Active Site | ACT_SITE 48; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000305|PubMed:19477183, ECO:0000305|PubMed:27594682" |
| 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:19477183, ECO:0000269|PubMed:27594682}; |
| 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. {ECO:0000269|PubMed:19477183}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Chain (1); Disulfide bond (1); Domain (1); Helix (7); Mutagenesis (2) |
| Keywords | 3D-structure;Antioxidant;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (17) |
| Cross Reference PDB | 3GKK; 3GKM; 3GKN; 5IM9; 5IMA; 5IMC; 5IMD; 5IMF; 5IMV; 5IMZ; 5INY; 5IO0; 5IO2; 5IOW; 5IOX; 5IPG; 5IPH; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 17,278 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=786 uM for H(2)O(2) {ECO:0000269|PubMed:27594682}; KM=1840 uM for cumene hydroperoxide {ECO:0000269|PubMed:27594682}; KM=293 uM for TrxA (using H(2)O(2) as substrate) {ECO:0000269|PubMed:27594682}; KM=414 uM for TrxA (using cumene hydroperoxide as substrate) {ECO:0000269|PubMed:27594682}; |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |