Reviewed,
UniProtKB/Swiss-Prot Q5HIR6 (AHPF_STAAC)
Last modified
June 16, 2009.
Version 32.
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 COL) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 93062 [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_0000166778 | |||||||
Regions | |||||||||||
| Nucleotide binding | 207 – 222 | 16 | FAD By similarity | ||||||||
| Nucleotide binding | 347 – 361 | 15 | NAD or NADP By similarity | ||||||||
| Nucleotide binding | 467 – 477 | 11 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 335 ↔ 338 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. Fraser C.M.J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000046 Genomic DNA. Translation: AAW38918.1. | |
| RefSeq | YP_185341.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3236479. |
| GenomeReviews | Gene locus SACOL0451 in contig CP000046_GR. |
| KEGG | sac:SACOL0451. |
| TIGR | SACOL0451. |
Phylogenomic databases | |
| HOGENOM | Q5HIR6. |
| OMA | Q5HIR6. ELEGVFV. |
Enzyme and pathway databases | |
| BioCyc | SAUR93062:SACOL0451-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_STAAC | ||||||||
| Accession | Primary (citable) accession number: Q5HIR6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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