ID AHPF_STAAR Reviewed; 507 AA.
AC Q6GJR8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE EC=1.8.1.-;
GN Name=ahpF; OrderedLocusNames=SAR0398;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains:
RT evidence for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Serves to protect the cell against DNA damage by alkyl
CC hydroperoxides. It can use either NADH or NADPH as electron donor
CC for direct reduction of redox dyes or of alkyl hydroperoxides when
CC combined with the AhpC protein (By similarity).
CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family.
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DR EMBL; BX571856; CAG39421.1; -; Genomic_DNA.
DR RefSeq; YP_039854.1; NC_002952.2.
DR ProteinModelPortal; Q6GJR8; -.
DR SMR; Q6GJR8; 205-507.
DR STRING; 282458.SAR0398; -.
DR EnsemblBacteria; CAG39421; CAG39421; SAR0398.
DR GeneID; 2860986; -.
DR KEGG; sar:SAR0398; -.
DR PATRIC; 19544312; VBIStaAur71814_0406.
DR eggNOG; COG3634; -.
DR HOGENOM; HOG000169462; -.
DR KO; K03387; -.
DR OMA; DQGPRFA; -.
DR ProtClustDB; PRK15317; -.
DR BioCyc; SAUR282458:GJA5-398-MONOMER; -.
DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR Gene3D; 3.40.30.10; -; 2.
DR InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000238; AhpF; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 2.
DR TIGRFAMs; TIGR03140; AhpF; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Disulfide bond; FAD; Flavoprotein; NAD; NADP;
KW Oxidoreductase; Redox-active center.
FT CHAIN 1 507 Alkyl hydroperoxide reductase subunit F.
FT /FTId=PRO_0000166781.
FT NP_BIND 207 222 FAD (By similarity).
FT NP_BIND 347 361 NAD or NADP (By similarity).
FT NP_BIND 467 477 FAD (By similarity).
FT DISULFID 335 338 Redox-active (By similarity).
SQ SEQUENCE 507 AA; 54693 MW; 9B2549AD9090EBC5 CRC64;
MLNADLKQQL KQLLELMEGN VEFVASLGSD DKSKELKELL TEISDMSPRL SLSEKSLKRT
PSFSVNRPGE ETGVTFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KNLEGSFHFE
TFISLTCQKC PDVVQALNLM SVINPNITHS MIDGAVFREE SENIMAVPAV FLNGEEFGNG
RMTIQDILSK LGSTADASEF ENKEPYDVLI VGGGPASGSA AIYTARKGLR TGIVADRIGG
QVNDTAGIEN FITVKETTGS EFSSNLAAHI DQYDIDAMTG IRATDIEKTD EAIKVTLENG
AVLESKTVII ATGAGWRKLN IPGEEQLINK GVAFCPHCDG PLFENKDVAV IGGGNSGVEA
AIDLAGIVNH VTLFEFASEL KADNVLQDRL RSLSNVDIKT NAKTTEVVGE NHVTGIRYED
MSTGEEHLLN LDGIFVQIGL LPNTSWLKDA VELNERGEIV IDRNNNTNVP GIFAAGDVTD
QKNKQIIISM GAGANAALNA FDYIIRN
//
