Q5HIR6 (AHPF_STAAC) 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:	SACOL0451

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.
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_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

	Sequence		Length	Mass (Da)
	Q5HIR6 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: EDED04232731D21E	FASTA	507	54,721
	10 20 30 40 50 60 MLNADLKQQL KQLLELMEGN VEFVASLGSD DKSKELKDLL TEITDMSPRL SLSEKSLKRT 70 80 90 100 110 120 PSFSVNRPGE ETGVTFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KKLEGSFHFE 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 MNTGEEHLLN LDGIFVQIGL LPNTSWLNDA VELNERGEIV IDRNNNTNVP GIFAAGDVTD 490 500 QKNKQIIISM GAGANAALNA FDYIIRN

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. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: COL.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000046 Genomic DNA. Translation: AAW38918.1.
RefSeq	YP_185341.1. NC_002951.2.
3D structure databases
ProteinModelPortal	Q5HIR6.
SMR	Q5HIR6. Positions 205-507.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HIR6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000009108; EBSTAP00000008843; EBSTAG00000009107.
GeneID	3236479.
GenomeReviews	Gene locus SACOL0451 in contig CP000046_GR.
KEGG	sac:SACOL0451.
PATRIC	19527142. VBIStaAur112458_0437.
TIGR	SACOL0451.
Phylogenomic databases
eggNOG	COG3634.
GeneTree	EBGT00050000023768.
HOGENOM	HBG289531.
OMA	MMAAINP.
ProtClustDB	PRK15317.
Enzyme and pathway databases
BioCyc	SAUR93062:SACOL0451-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_STAAC

Accession

Primary (citable) accession number: Q5HIR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program