Reviewed,
UniProtKB/Swiss-Prot Q6UBI3 (PERQ_SUASA)
Last modified
November 25, 2008.
Version 38.
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 |
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| Organism | Suaeda salsa (Seepweed) (Chenopodium salsum) | ||
| Taxonomic identifier | 126914 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Suaeda |
Protein attributes
| Sequence length | 214 AA. |
| Sequence status | Complete. |
| 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' + H(2)O + ROH. |
| Subunit structure | Monomer. |
| Subcellular location | Plastid › chloroplast thylakoidBy similarity. |
| Induction | Up-regulated by NaCl, mannitol, low temperature, H(2)O(2), methyl viologen, and abscisic acid (ABA). |
| Post-translational modification | The Cys-109-SH group is the primary site of oxidation by H(2)O(2), and the oxidized Cys-109 (probably Cys-SOH) rapidly reacts with Cys-114-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 |
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 Inferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 64 | 64 | Chloroplast Potential | ||||||||
| Chain | 65 – 214 | 150 | Peroxiredoxin Q, chloroplastic | PRO_0000285113 | |||||||
Regions | |||||||||||
| Domain | 67 – 214 | 148 | Thioredoxin | ||||||||
Sites | |||||||||||
| Active site | 109 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 109 ↔ 114 | Redox-active | |||||||||
Sequences
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References
| [1] | "Molecular cloning and characterization of a stress-induced peroxiredoxin Q gene in halophyte Suaeda salsa." Guo X.-L., Cao Y.-R., Cao Z.-Y., Zhao Y.-X., Zhang H. Plant Sci. 167:969-975(2004) [Agricola: IND43645556] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. |
Cross-references
Sequence databases | |
|---|---|
| AY373447 mRNA. Translation: AAQ67661.1. | |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 4306. SsaPrxQ. |
Family and domain databases | |
| InterPro | IPR000866. AhpC-TSA. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF00578. AhpC-TSA. 1 hit. [Graphical view] |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PERQ_SUASA | ||||||||
| Accession | Primary (citable) accession number: Q6UBI3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

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