Q6GC92 (AHPF_STAAS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkyl hydroperoxide reductase subunit F
EC=1.8.1.-

Gene names

Name:	ahpF
Ordered Locus Names:	SAS0357

Organism

Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]

Taxonomic identifier

282459 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
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
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on NADH or NADPH Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred 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_0000166782
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

	Sequence		Length	Mass (Da)
	Q6GC92 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 636669352789C552	FASTA	507	54,655
	10 20 30 40 50 60 MLNADLKQQL KQLLELMEGN VEFVASLGSD EKSKELKELL TEISDMSPRL SLSEKSLKRT 70 80 90 100 110 120 PSFSVNRPGE ETGVTFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KNLEGSFHFE 130 140 150 160 170 180 TFISLTCQKC PDVVQALNLM SVINPNITHS MIDGAVFREE SENIMAVPAV FLNGEEFGNG 190 200 210 220 230 240 RMTIQDILSK LGSTADASEF ENKEPYDVLI VGGGPASGSA AIYTARKGLR TGIVADRIGG 250 260 270 280 290 300 QVNDTAGIEN FITVKETTGS EFSSNLAAHI DQYDIDAMTG IRATDIEKTD EAIKVTLENG 310 320 330 340 350 360 AVLESKTVII ATGAGWRKLN IPGEEQLINK GVAFCPHCDG PLFENKDVAV IGGGNSGVEA 370 380 390 400 410 420 AIDLAGIVNH VTLFEFASEL KADNVLQDRL RSLSNVDIKT NAKTTEVVGE DHVTGIRYED 430 440 450 460 470 480 MSTGEEHLLN LDGIFVQIGL LPNTSWLKDA VELNERGEIV IDCNNNTNVP GIFAAGDVTD 490 500 QKNKQIIISM GAGANAALNA FDYIIRN

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MSSA476.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571857 Genomic DNA. Translation: CAG42128.1.
RefSeq	YP_042481.1. NC_002953.3.
3D structure databases
ProteinModelPortal	Q6GC92.
SMR	Q6GC92. Positions 205-507.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6GC92.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000023569; EBSTAP00000022736; EBSTAG00000023568.
GeneID	2864304.
GenomeReviews	Gene locus SAS0357 in contig BX571857_GR.
KEGG	sas:SAS0357.
PATRIC	19550074. VBIStaAur96780_0375.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3634.
GeneTree	EBGT00050000023768.
HOGENOM	HBG289531.
OMA	MMAAINP.
ProtClustDB	PRK15317.
Enzyme and pathway databases
BioCyc	SAUR282459:SAS0357-MONOMER.
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. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
KO	K03387.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PIRSF	PIRSF000238. AhpF. 1 hit.
PRINTS	PR00368. FADPNR. PR00469. PNDRDTASEII.
SUPFAM	SSF52833. Thiordxn-like_fd. 2 hits.
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_STAAS

Accession

Primary (citable) accession number: Q6GC92

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program