Q9ZHF0 · BCP_BUCAP
- ProteinPutative peroxiredoxin bcp
- Genebcp
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids158 (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 and as sensor of hydrogen peroxide-mediated signaling events.
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 | 46 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | thioredoxin peroxidase activity | |
Biological Process | cell redox homeostasis | |
Biological Process | cellular response to oxidative stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative peroxiredoxin bcp
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Buchnera
Accessions
- Primary accessionQ9ZHF0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000135133 | 1-158 | Putative peroxiredoxin bcp | |||
Sequence: MTTLKPGDIAPKFILPNCIDKSIKLSDFLGKKVLVYFYPKAMTPGCTVQACNIRDNLELFKSKKVEVLGISPDNTNKLLTFVEKKMLNFTLLSDKQNIVSKKFGVWGEKIFMGKKYFGIYRTSFLINSSGFIDKIFFKFKCKDHHKIILTYLNSKKSD | ||||||
Disulfide bond | 46↔51 | Redox-active | ||||
Sequence: CTVQAC |
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-157 | Thioredoxin | ||||
Sequence: LKPGDIAPKFILPNCIDKSIKLSDFLGKKVLVYFYPKAMTPGCTVQACNIRDNLELFKSKKVEVLGISPDNTNKLLTFVEKKMLNFTLLSDKQNIVSKKFGVWGEKIFMGKKYFGIYRTSFLINSSGFIDKIFFKFKCKDHHKIILTYLNSKKS |
Sequence similarities
Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length158
- Mass (Da)18,138
- Last updated2002-08-30 v2
- Checksum7D06D4025FF297B5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013218 EMBL· GenBank· DDBJ | AAM67659.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF067228 EMBL· GenBank· DDBJ | AAC97351.1 EMBL· GenBank· DDBJ | Genomic DNA |