(data stored in ACNUC7421 zone)

SWISSPROT: B7UKQ0_ECO27

ID   B7UKQ0_ECO27            Unreviewed;       521 AA.
AC   B7UKQ0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   SubName: Full=Alkyl hydroperoxide reductase, F52a subunit, FAD/NAD(P)-binding {ECO:0000313|EMBL:CAS08057.1};
GN   Name=ahpF {ECO:0000313|EMBL:CAS08057.1};
GN   OrderedLocusNames=E2348C_0509 {ECO:0000313|EMBL:CAS08057.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08057.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08057.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FM180568; CAS08057.1; -; Genomic_DNA.
DR   RefSeq; WP_012578846.1; NC_011601.1.
DR   EnsemblBacteria; CAS08057; CAS08057; E2348C_0509.
DR   KEGG; ecg:E2348C_0509; -.
DR   HOGENOM; HOG000169462; -.
DR   KO; K03387; -.
DR   OMA; VPLGHEF; -.
DR   BioCyc; ECOL574521:E2348C_RS02675-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UKQ0.
DR   SWISS-2DPAGE; B7UKQ0.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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;  56207 MW;  6CBD0846036755B3 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
     GLHQIETTSG AVLKARSIIV ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV
     IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKL RSLKNVDIIL NAQTTEVKGD
     GSKVVGLEYR DRVSGDIHNI ELAGIFVQIG LLPNTNWLEG AVERNRMGEI IIDAKCETNV
     KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKT A
//

If you have problems or comments...

PBIL Back to PBIL home page