IED ID | IndEnz0018001338 |
Enzyme Type ID | peroxidase001338 |
Protein Name |
Putative peroxiredoxin prxA Prx EC 1.11.1.24 Thioredoxin peroxidase TPx Thioredoxin-dependent peroxiredoxin |
Gene Name | prxA PRX5 AN8692 |
Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Enzyme Sequence | MSGLKAGDSFPADVVFSYIPWTEEKGEITSCGIPINYYASKEWADKKVILFALPGAFTPVCSARHVPEYIERLPEIRAKGVDVVAVLAYNDAFVMSAWGKANGVKNDDILFLSDPEAKFSKSIGWADEEGRTKRYAIVLDHGKVTYAALEPAKNHLEFSSAETVIKHL |
Enzyme Length | 168 |
Uniprot Accession Number | Q5ASN8 |
Absorption | |
Active Site | ACT_SITE 61; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000305|PubMed:19965775 |
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:17631497}; |
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). Involved in osmoadaptation (PubMed:17258477). {ECO:0000250|UniProtKB:O43099, ECO:0000250|UniProtKB:P38013, ECO:0000269|PubMed:17258477}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1) |
Keywords | Antioxidant;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome;Stress response |
Interact With | |
Induction | INDUCTION: Down-regulated when grown with elevated levels of potassium chloride (PubMed:17258477). Induced under oxidative stress conditions dependent on transcription factor napA (PubMed:19965775). {ECO:0000269|PubMed:17258477, ECO:0000269|PubMed:19965775}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 18,527 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 uM for H(2)O(2) {ECO:0000269|PubMed:17631497}; Vmax=6.8 umol/min/mg enzyme {ECO:0000269|PubMed:17631497}; |
Metal Binding | |
Rhea ID | RHEA:62620 |
Cross Reference Brenda |