IED ID | IndEnz0018001146 |
Enzyme Type ID | peroxidase001146 |
Protein Name |
Glutathione peroxidase-like peroxiredoxin GPX3 EC 1.11.1.24 Glutathione peroxidase homolog 3 GPx 3 |
Gene Name | GPX3 CAALFM_C107350CA orf19.4436 |
Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
Enzyme Sequence | MGNELLSTARIYTFKIPDAYNNVIDFDQFKNKVILIVNVASLCGFTPQYKELQLLYEKYHERGLEILGFPCNQFGNQEPLQEEEIVESCRRNFGVSFPIMKKTKVNIDCDGHESELYKYLKSEKPGEVGFKGVRWNFEKFIVNRKGEVVARFNSLITPLQLEGFIEQLLSE |
Enzyme Length | 171 |
Uniprot Accession Number | Q59WD3 |
Absorption | |
Active Site | ACT_SITE 43; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P40581 |
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:P40581}; |
DNA Binding | |
EC Number | 1.11.1.24 |
Enzyme Function | FUNCTION: Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator CAP1, which is involved in transcription activation of genes of the oxidative stress response pathway (PubMed:23706023). May also play a direct role in hydroperoxide scavenging. The enzyme is not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, GPX3 is directly oxidized at Cys-43 to form a cysteine sulfenic acid (-SOH). Cys-43-SOH then forms either an intramolecular disulfide bond (Cys-43 with Cys-89) or a transient, intermolecular disulfide bond with 'Cys-446' of CAP1, which is further resolved into a CAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598'), which causes its nuclear accumulation and activation, and a reduced Cys-43 in GPX3 (By similarity). Required for C.albicans-mediated macrophage killing (PubMed:23706023). {ECO:0000250|UniProtKB:P40581, ECO:0000269|PubMed:23706023}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (2) |
Keywords | Antioxidant;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 19,842 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:62620 |
Cross Reference Brenda |