| IED ID | IndEnz0018001373 |
| Enzyme Type ID | peroxidase001373 |
| Protein Name |
Hybrid peroxiredoxin hyPrx5 EC 1.11.1.27 Glutathione-dependent peroxidase Glutathione-dependent peroxiredoxin Peroxiredoxin-glutaredoxin fusion protein PGdx Prx-Grx |
| Gene Name | PGdx HI_0572 |
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Haemophilus Haemophilus influenzae Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Enzyme Sequence | MSSMEGKKVPQVTFRTRQGDKWVDVTTSELFDNKTVIVFSLPGAFTPTCSSSHLPRYNELAPVFKKYGVDDILVVSVNDTFVMNAWKEDEKSENISFIPDGNGEFTEGMGMLVGKEDLGFGKRSWRYSMLVKNGVVEKMFIEPNEPGDPFKVSDADTMLKYLAPQHQVQESISIFTKPGCPFCAKAKQLLHDKGLSFEEIILGHDATIVSVRAVSGRTTVPQVFIGGKHIGGSDDLEKYFA |
| Enzyme Length | 241 |
| Uniprot Accession Number | P44758 |
| Absorption | |
| Active Site | ACT_SITE 49; /note=Cysteine sulfenic acid (-SOH) intermediate; for peroxiredoxin activity; /evidence=ECO:0000305|PubMed:12606554 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000269|PubMed:12606554, ECO:0000269|Ref.3}; |
| DNA Binding | |
| EC Number | 1.11.1.27 |
| 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:12606554, ECO:0000269|Ref.3}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8. {ECO:0000269|PubMed:12606554}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (15); Chain (1); Disulfide bond (1); Domain (2); Helix (9); Turn (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 (1) |
| Cross Reference PDB | 1NM3; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,743 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.29 uM for H(2)O(2) {ECO:0000269|PubMed:12606554}; KM=208.8 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:12606554}; Vmax=25.74 umol/min/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:12606554}; Vmax=26.57 umol/min/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:12606554}; |
| Metal Binding | |
| Rhea ID | RHEA:62632 |
| Cross Reference Brenda | 1.11.1.27; |