(data stored in SCRATCH zone)

SWISSPROT: C8U2X1_ECO10

ID   C8U2X1_ECO10            Unreviewed;       521 AA.
AC   C8U2X1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   SubName: Full=Alkyl hydroperoxide reductase, F52a subunit, FAD /NAD(P)-binding {ECO:0000313|EMBL:BAI29479.1};
GN   Name=ahpF {ECO:0000313|EMBL:BAI29479.1};
GN   OrderedLocusNames=ECO103_0615 {ECO:0000313|EMBL:BAI29479.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29479.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29479.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000238-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000238-1};
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DR   EMBL; AP010958; BAI29479.1; -; Genomic_DNA.
DR   RefSeq; WP_000887629.1; NC_013353.1.
DR   SMR; C8U2X1; -.
DR   EnsemblBacteria; BAI29479; BAI29479; ECO103_0615.
DR   KEGG; eoh:ECO103_0615; -.
DR   HOGENOM; HOG000169462; -.
DR   KO; K03387; -.
DR   OMA; VPLGHEF; -.
DR   BioCyc; ECOL585395:ECO103_RS03205-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer 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; 3.50.50.60; -; 2.
DR   InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   TIGRFAMs; TIGR03140; AhpF; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   4: Predicted;
DR   PRODOM; C8U2X1.
DR   SWISS-2DPAGE; C8U2X1.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000238-2};
KW   FAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000238-1};
KW   NAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW   NADP {ECO:0000256|PIRSR:PIRSR000238-1};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR000238-2}.
FT   DOMAIN      109    211       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
FT   NP_BIND     214    229       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   NP_BIND     357    371       NAD or NADP. {ECO:0000256|PIRSR:
FT                                PIRSR000238-1}.
FT   NP_BIND     478    488       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   COILED       36     56       {ECO:0000256|SAM:Coils}.
FT   DISULFID    345    348       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000238-2}.
SQ   SEQUENCE   521 AA;  56177 MW;  F39C50F922395B48 CRC64;
     MLDTNMKTQL KAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNSLPV
     RKPSFLITNP GSNQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRHIDGDFE
     FETYYSLSCH NCPDVVQALN LMSVLNPRIK HTAIDGGTFQ NEITDRNVMG VPAVFVNGKE
     FGQGRMTLTE IVAKIDTGAE KRAAEELNKR DAYDVLIVGS GPAGAAAAIY SARKGIRTGL
     MGERFGGQIL DTVDIENYIS VPKTEGQKLA GALKVHVDEY DVDVIDSQSA SKLIPAAVEG
     GLHQIETASG AVLKARSIIV ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV
     IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKL RSLKNVDIIL NAQTTEVKGD
     GSKVVGLEYR DRVSGDIHNI ELAGIFVQIG LLPNTNWLEG AVERNRMGEI IIDAKCETNV
     KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKT A
//

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