(data stored in SCRATCH zone)

SWISSPROT: B7UKP9_ECO27

ID   B7UKP9_ECO27            Unreviewed;       187 AA.
AC   B7UKP9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|RuleBase:RU366004};
DE            EC=1.11.1.15 {ECO:0000256|RuleBase:RU366004};
DE   AltName: Full=Peroxiredoxin {ECO:0000256|RuleBase:RU366004};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|RuleBase:RU366004};
GN   Name=ahpC {ECO:0000313|EMBL:CAS08056.1};
GN   OrderedLocusNames=E2348C_0508 {ECO:0000313|EMBL:CAS08056.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08056.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08056.1, 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   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
CC       of hydrogen peroxide and organic hydroperoxides to water and
CC       alcohols, respectively. Plays a role in cell protection against
CC       oxidative stress by detoxifying peroxides.
CC       {ECO:0000256|RuleBase:RU366004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
CC         + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC         EC=1.11.1.15; Evidence={ECO:0000256|RuleBase:RU366004};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU366004}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
CC       subfamily. {ECO:0000256|RuleBase:RU366004}.
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DR   EMBL; FM180568; CAS08056.1; -; Genomic_DNA.
DR   RefSeq; WP_000052796.1; NC_011601.1.
DR   SMR; B7UKP9; -.
DR   EnsemblBacteria; CAS08056; CAS08056; E2348C_0508.
DR   KEGG; ecg:E2348C_0508; -.
DR   HOGENOM; HOG000022343; -.
DR   KO; K03386; -.
DR   OMA; WYPKDFT; -.
DR   BioCyc; ECOL574521:E2348C_RS02670-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR   InterPro; IPR017559; AhpC.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF121; PTHR10681:SF121; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR03137; AhpC; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKP9.
DR   SWISS-2DPAGE; B7UKP9.
KW   Antioxidant {ECO:0000256|RuleBase:RU366004};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|RuleBase:RU366004};
KW   Disulfide bond {ECO:0000256|RuleBase:RU366004};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366004};
KW   Peroxidase {ECO:0000256|RuleBase:RU366004};
KW   Redox-active center {ECO:0000256|RuleBase:RU366004}.
FT   DOMAIN        2    157       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   ACT_SITE     47     47       Cysteine sulfenic acid (-SOH)
FT                                intermediate. {ECO:0000256|PIRSR:
FT                                PIRSR000239-1}.
SQ   SEQUENCE   187 AA;  20761 MW;  40AB796E6F5CC2D6 CRC64;
     MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE
     LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR
     ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS
     LDLVGKI
//

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