F4G1K5 · F4G1K5_METCR
- ProteinPeroxiredoxin
- StatusUniProtKB unreviewed (TrEMBL)
- 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 | 46 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C | ||||||
Active site | 46 | Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity | ||||
Sequence: C | ||||||
Binding site | 121 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | thioredoxin peroxidase activity | |
Biological Process | cell redox homeostasis | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
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 > Metallosphaera
Accessions
- Primary accessionF4G1K5
Proteomes
Subcellular Location
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 | 2-158 | Thioredoxin | ||||
Sequence: VKTYQKFPDVQVMTTAGPIDFYKDVFGKGKWLFLFAHPADFTPVCTTEFVEFAKNYSEFEKLGVQLVGLSVDSIYSHIAWLTDIEQRYGVKIPFPVIADPDKKIARLLDLIEEGSGLTVRGVFIVDPQGTIRFMALYPIEAGRNMQELIRITKALIV |
Sequence similarities
Belongs to the peroxiredoxin family. Prx6 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length215
- Mass (Da)24,469
- Last updated2011-06-28 v1
- Checksum908708484D2579F7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002656 EMBL· GenBank· DDBJ | AEB94818.1 EMBL· GenBank· DDBJ | Genomic DNA |