P0C5C8 · REHYA_ORYSI
- Protein1-Cys peroxiredoxin A
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids220 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity).
Seems to contribute to the inhibition of germination during stress (By similarity).
Seems to contribute to the inhibition of germination during stress (By similarity).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 46 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | thioredoxin-dependent peroxiredoxin activity |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended name1-Cys peroxiredoxin A
- EC number
- Short names1-Cys Prx A
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionP0C5C8
- Secondary accessions
Proteomes
Genome annotation databases
Phenotypes & Variants
Protein family/group databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000300260 | 1-220 | 1-Cys peroxiredoxin A | |||
Sequence: MPGLTIGDTVPNLELDSTHGKIRIHDFVGDTYIILFSHPGDFTPVCTTELAAMAGYAKEFDKRGVKLLGISCDDVQSHKDWIKDIEAYKPGNRVTYPIMADPSREAIKQLNMVDPDEKDSNGGHLPSRALHIVGPDKKVKLSFLYPSCVGRNMDEVVRAVDALQTAAKHAVATPVNWKPGERVVIPPGVSDDEAKEKFPQGFDTADLPSGKGYLRFTKVG |
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-165 | Thioredoxin | ||||
Sequence: LTIGDTVPNLELDSTHGKIRIHDFVGDTYIILFSHPGDFTPVCTTELAAMAGYAKEFDKRGVKLLGISCDDVQSHKDWIKDIEAYKPGNRVTYPIMADPSREAIKQLNMVDPDEKDSNGGHLPSRALHIVGPDKKVKLSFLYPSCVGRNMDEVVRAVDALQT | ||||||
Motif | 195-218 | Bipartite nuclear localization signal | ||||
Sequence: KEKFPQGFDTADLPSGKGYLRFTK |
Sequence similarities
Belongs to the peroxiredoxin family. Prx6 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length220
- Mass (Da)24,072
- Last updated2007-09-11 v1
- Checksum317D9D76C7D63F1D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM000132 EMBL· GenBank· DDBJ | EEC82522.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CT830870 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |