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Database: UniProt
Entry: Q6GJR8
LinkDB: Q6GJR8
Original site: Q6GJR8 
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   26-NOV-2014, entry version 71.
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). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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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   OrthoDB; EOG65XN2W; -.
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; SSF52833; 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. {ECO:0000250}.
FT   NP_BIND     347    361       NAD or NADP. {ECO:0000250}.
FT   NP_BIND     467    477       FAD. {ECO:0000250}.
FT   DISULFID    335    338       Redox-active. {ECO:0000250}.
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
//
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