Reviewed,
UniProtKB/Swiss-Prot P0AE09 (AHPC_ECOL6)
Last modified
June 16, 2009.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alkyl hydroperoxide reductase subunit C EC=1.11.1.15 Alternative name(s): Peroxiredoxin Thioredoxin peroxidase Alkyl hydroperoxide reductase protein C22 SCRP-23 Sulfate starvation-induced protein 8 Short name=SSI8 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 187 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Directly reduces organic hydroperoxides in its reduced dithiol form By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Homodimer; disulfide-linked, upon oxidation By similarity. |
| Post-translational modification | The Cys-47-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-47 (probably Cys-SOH) rapidly reacts with Cys-166-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin By similarity. |
| Sequence similarities | Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Domain | Redox-active center |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
| PTM | Acetylation Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 187 | 186 | Alkyl hydroperoxide reductase subunit C | PRO_0000135117 | |||||
Regions | |||||||||
| Domain | 2 – 157 | 156 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 47 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 17 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 93 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 153 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 169 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 171 | 1 | N6-acetyllysine By similarity | ||||||
| Disulfide bond | 47 | Interchain (with C-166); in linked form By similarity | |||||||
| Disulfide bond | 166 | Interchain (with C-47); in linked form By similarity | |||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| AE014075 Genomic DNA. Translation: AAN79169.1. | |
| RefSeq | NP_752625.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N8J based on UniProtKB P19479. |
| SMR | P0AE09. Positions 2-187. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1035753. |
| GenomeReviews | Gene locus c0694 in contig AE014075_GR. |
| KEGG | ecc:c0694. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0AE09. |
| OMA | P0AE09. GDLADHY. |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.15. 292881. |
Family and domain databases | |
| InterPro | IPR000866. Alkyl_hydroperoxide_Rdtase. IPR017559. Peroxiredoxin. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03137. AhpC. 1 hit. |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AHPC_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0AE09 Secondary accession number(s): P26427 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


