(data stored in SCRATCH zone)

SWISSPROT: C8U2X0_ECO10

ID   C8U2X0_ECO10            Unreviewed;       187 AA.
AC   C8U2X0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-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:BAI29478.1};
GN   OrderedLocusNames=ECO103_0614 {ECO:0000313|EMBL:BAI29478.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29478.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29478.1, 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   -!- 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; AP010958; BAI29478.1; -; Genomic_DNA.
DR   RefSeq; WP_000052796.1; NC_013353.1.
DR   SMR; C8U2X0; -.
DR   EnsemblBacteria; BAI29478; BAI29478; ECO103_0614.
DR   KEGG; eoh:ECO103_0614; -.
DR   HOGENOM; HOG000022343; -.
DR   KO; K03386; -.
DR   OMA; WYPKDFT; -.
DR   BioCyc; ECOL585395:ECO103_RS03200-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U2X0.
DR   SWISS-2DPAGE; C8U2X0.
KW   Antioxidant {ECO:0000256|RuleBase:RU366004};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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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