(data stored in SCRATCH zone)

SWISSPROT: Q3Z4I7_SHISS

ID   Q3Z4I7_SHISS            Unreviewed;       531 AA.
AC   Q3Z4I7;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 104.
DE   SubName: Full=Alkyl hydroperoxide reductase, F52a subunit {ECO:0000313|EMBL:AAZ87325.1};
GN   Name=ahpF {ECO:0000313|EMBL:AAZ87325.1};
GN   OrderedLocusNames=SSON_0558 {ECO:0000313|EMBL:AAZ87325.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87325.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87325.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87325.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87325.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87325; AAZ87325; SSON_0558.
DR   KEGG; ssn:SSON_0558; -.
DR   HOGENOM; HOG000169462; -.
DR   KO; K03387; -.
DR   OMA; VPLGHEF; -.
DR   Proteomes; UP000002529; 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; Q3Z4I7.
DR   SWISS-2DPAGE; Q3Z4I7.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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      119    221       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
FT   NP_BIND     224    239       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   NP_BIND     367    381       NAD or NADP. {ECO:0000256|PIRSR:
FT                                PIRSR000238-1}.
FT   NP_BIND     488    498       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   COILED       46     66       {ECO:0000256|SAM:Coils}.
FT   DISULFID    355    358       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000238-2}.
SQ   SEQUENCE   531 AA;  57402 MW;  93D5A721D38353A5 CRC64;
     MMMFKAQEIN 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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