P95895 · TDXH_SACS2
- ProteinPeroxiredoxin
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids215 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Miscellaneous
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule.
Catalytic activity
- [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ CHEBI:35924 = RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:30879 + CHEBI:15377
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 49 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C | ||||||
Binding site | 125 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | thioredoxin-dependent peroxiredoxin activity | |
Biological Process | cell redox homeostasis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxiredoxin
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Saccharolobus
Accessions
- Primary accessionP95895
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000135169 | 1-215 | Peroxiredoxin | |||
Sequence: MSEERIPLIGERFPEMEVITTQGRIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWIMWIEKNLKVEIPFPIIADPMGNVAKRLGMIHAQSSTATVRAVFVVDDKGVVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANWPNNELIGDKVINPAPRTIKDAKMRLGQPFDWWFTYKEVKTT |
Proteomic databases
Interaction
Subunit
Homodecamer. Pentamer of dimers that assemble into a ring structure.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-162 | Thioredoxin | ||||
Sequence: PLIGERFPEMEVITTQGRIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWIMWIEKNLKVEIPFPIIADPMGNVAKRLGMIHAQSSTATVRAVFVVDDKGVVRLILYYPMEIGRNIDEILRAIRALQL |
Sequence similarities
Belongs to the peroxiredoxin family. Prx6 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length215
- Mass (Da)24,745
- Last updated1997-05-01 v1
- Checksum5210477EF4C9607B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y08256 EMBL· GenBank· DDBJ | CAA69447.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006641 EMBL· GenBank· DDBJ | AAK42300.1 EMBL· GenBank· DDBJ | Genomic DNA |