IED ID | IndEnz0018001601 |
Enzyme Type ID | peroxidase001601 |
Protein Name |
Peroxiredoxin TSA1-A EC 1.11.1.24 Thiol-specific antioxidant protein Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin TSA1-A |
Gene Name | TSA1 TSA1A CAALFM_C306180CA CaO19.7417 |
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 | MAPVVQQPAPSFKKTAVVDGVFEEVTLEQYKGKWVLLAFIPLAFTFVCPSEIIAYSEAVKKFAEKDAQVLFASTDSEYTWLAWTNVARKDGGIGKVDFPVLADTNHSLSRDYGVLIEEEGVALRGIFLIDPKGVLRQITINDLPVGRSVEESLRLLEAFQFTEKYGEVCPANWHPGDETIKPSPEASKEYFNKVNK |
Enzyme Length | 196 |
Uniprot Accession Number | Q9Y7F0 |
Absorption | |
Active Site | ACT_SITE 48; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P34760 |
Activity Regulation | |
Binding Site | BINDING 124; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P34760 |
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:P34760}; |
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. Also involved in the correct composition of the hyphal cell wall. {ECO:0000269|PubMed:16102003}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Domain (1); Region (2) |
Keywords | Antioxidant;Cytoplasm;Disulfide bond;Nucleus;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
Interact With | |
Induction | INDUCTION: Induced by oxidative stress. {ECO:0000269|PubMed:16102003}. |
Subcellular Location | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:12782322, ECO:0000269|PubMed:16102003}. Nucleus {ECO:0000269|PubMed:12782322, ECO:0000269|PubMed:16134099}. Cytoplasm {ECO:0000269|PubMed:12782322, ECO:0000269|PubMed:16134099}. Note=Localizes to the cell surface in hyphally grown cells, whereas no surface but mainly nuclear localization is found in yeast-form cells. {ECO:0000269|PubMed:12782322, ECO:0000269|PubMed:16102003}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 21,860 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:62620 |
Cross Reference Brenda |