A0A443ZEC5 · A0A443ZEC5_9PSED
- ProteinThiol peroxidase
- Genetpx
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids166 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 60 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | thioredoxin peroxidase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThiol peroxidase
- EC number
- Short namesTpx
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A443ZEC5
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 60↔94 | Redox-active | ||||
Sequence: CATSVRTFNKKAGELNNTVVLCISADLPFAQARFC |
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-166 | Thioredoxin | ||||
Sequence: PKVGAKAPAFSLVGAGLADVTLASLAGKRKVLNIFPSVDTPTCATSVRTFNKKAGELNNTVVLCISADLPFAQARFCGAEGLENVQNLSTLRGREFIENYGVAIADGPLAGLTARAVVVLDENDTVLHSELVGEIADEPNYDAALAVLK |
Sequence similarities
Belongs to the peroxiredoxin family. Tpx subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length166
- Mass (Da)17,305
- Last updated2019-05-08 v1
- Checksum8D231A9BF857B0B2