Reviewed,
UniProtKB/Swiss-Prot O05204 (AHPF_STAA8)
Last modified
June 16, 2009.
Version 65.
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 F EC=1.6.4.- | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain NCTC 8325) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 93061 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 507 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the ahpC protein By similarity. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Miscellaneous | The active site is a redox-active disulfide bond. |
| Sequence similarities | Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD NADP |
| Molecular function | Oxidoreductase |
| PTM | 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 | FAD binding Inferred from electronic annotation. Source: InterPro NAD or NADH bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on NADH or NADPHInferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 507 | 507 | Alkyl hydroperoxide reductase subunit F | PRO_0000166784 | |||||||
Regions | |||||||||||
| Nucleotide binding | 207 – 222 | 16 | FAD (ADP part) By similarity | ||||||||
| Nucleotide binding | 347 – 361 | 15 | NAD or NADP By similarity | ||||||||
| Nucleotide binding | 467 – 477 | 11 | FAD (pyrimidine part) By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 335 ↔ 338 | Redox-active By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Jones E.C., Francis K.P., Stewart G.S.A.B. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| U92441 Genomic DNA. Translation: AAB51152.1. CP000253 Genomic DNA. Translation: ABD29530.1. | |
| RefSeq | YP_498953.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FL2 based on UniProtKB P35340. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3919783. |
| GenomeReviews | Gene locus SAOUHSC_00364 in contig CP000253_GR. |
| KEGG | sao:SAOUHSC_00364. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O05204. |
| OMA | O05204. ELEGVFV. |
Enzyme and pathway databases | |
| BioCyc | SAUR93061:SAOUHSC_00364-MON. |
Family and domain databases | |
| InterPro | IPR012081. Alkyl_hydroperoxide_Rdtase_suF. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR002109. Glutaredoxin. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000238. AhpF. 1 hit. |
| PRINTS | PR00368. FADPNR. PR00469. PNDRDTASEII. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR03140. AhpF. 1 hit. |
| PROSITE | PS51354. GLUTAREDOXIN_2. 1 hit. PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AHPF_STAA8 | ||||||||
| Accession | Primary (citable) accession number: O05204 Secondary accession number(s): Q2G0Z7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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