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 |