A0A2N0XI81 · A0A2N0XI81_9FLAO
- ProteinThiol peroxidase
- Genetpx
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids190 (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 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
- a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O
CHEBI:35924 + RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3= CHEBI:30879 + RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:15377
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 84 | Cysteine sulfenic acid (-SOH) intermediate | |||
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 > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium
Accessions
- Primary accessionA0A2N0XI81
Proteomes
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-19 | ||||
Chain | PRO_5014884020 | 20-190 | Thiol peroxidase | ||
Disulfide bond | 84↔118 | Redox-active | |||
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length190
- Mass (Da)21,043
- Last updated2018-04-25 v1
- ChecksumD9B175E65AAB2726
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PIZV01000012 EMBL· GenBank· DDBJ | PKF75658.1 EMBL· GenBank· DDBJ | Genomic DNA |