Reviewed,
UniProtKB/Swiss-Prot Q9MB35 (PERQ_SEDLI)
Last modified
June 16, 2009.
Version 36.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peroxiredoxin Q, chloroplastic EC=1.11.1.15 Alternative name(s): Thioredoxin reductase | ||
| Gene names |
| ||
| Organism | Sedum lineare (Needle stonecrop) | ||
| Taxonomic identifier | 114260 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Saxifragales › Crassulaceae › Sedum |
Protein attributes
| Sequence length | 186 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Reduces hydrogen peroxide with reducing equivalents provided through the thioredoxin system By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Monomer. Ref.1 |
| Subcellular location | Plastid › chloroplast thylakoid By similarity. |
| Post-translational modification | The Cys-80-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-80 (probably Cys-SOH) rapidly reacts with Cys-85-SH to form an intramolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme. |
| Sequence similarities | Belongs to the ahpC/TSA family. PrxQ subfamily. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chloroplast Plastid |
| Domain | Redox-active center Transit peptide |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast thylakoid Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | peroxiredoxin activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | ‹1 – 36 | ›36 | Chloroplast Potential | ||||||||
| Chain | 37 – 186 | 150 | Peroxiredoxin Q, chloroplastic | PRO_5000049527 | |||||||
Regions | |||||||||||
| Domain | 38 – 186 | 149 | Thioredoxin | ||||||||
Sites | |||||||||||
| Active site | 80 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 80 ↔ 85 | Redox-active | |||||||||
Experimental info | |||||||||||
| Non-terminal residue | 1 | 1 | |||||||||
Sequences
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References
| [1] | "A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)." Kong W., Shiota S., Shi Y., Nakayama H., Nakayama K. Biochem. J. 351:107-114(2000) [PubMed: 10998352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT. |
Cross-references
Sequence databases | |
|---|---|
| AB037598 mRNA. Translation: BAA90524.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QQ2 based on UniProtKB Q63716. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 4304. SlinPrxQ. |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.15. 291237. |
Family and domain databases | |
| InterPro | IPR000866. Alkyl_hydroperoxide_Rdtase. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF00578. AhpC-TSA. 1 hit. [Graphical view] |
| ProDom | PD003679. Thioredoxin_like. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PERQ_SEDLI | ||||||||
| Accession | Primary (citable) accession number: Q9MB35 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


