(data stored in ACNUC1104 zone)

SWISSPROT: B1K206_BURCC

ID   B1K206_BURCC            Unreviewed;       187 AA.
AC   B1K206;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 57.
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   OrderedLocusNames=Bcenmc03_3432 {ECO:0000313|EMBL:ACA92585.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92585.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000959; ACA92585.1; -; Genomic_DNA.
DR   RefSeq; WP_011547973.1; NC_010515.1.
DR   EnsemblBacteria; ACA92585; ACA92585; Bcenmc03_3432.
DR   KEGG; bcm:Bcenmc03_3432; -.
DR   HOGENOM; HOG000022343; -.
DR   KO; K03386; -.
DR   OMA; WYPKDFT; -.
DR   BioCyc; BCEN406425:G1GBC-3644-MONOMER; -.
DR   Proteomes; UP000002169; Chromosome 2.
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; B1K206.
DR   SWISS-2DPAGE; B1K206.
KW   Antioxidant {ECO:0000256|RuleBase:RU366004};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
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;  20725 MW;  14165C91515FAE31 CRC64;
     MPIINTQIKP FKATAYHNGE FVPVSEENFK GKWSVVVFYP ADFTFVCPTE LGDLADRYAE
     FQKLGVEIYG VSTDTHFTHK AWHDTSDTIA KIKYPLVGDP TLTLSRNFDV LIEEEGMALR
     GTFVINPEGE IKLCEIHDNG IGRDAGELLR KVQAAQYIAA HPGEVCPAKW TPGAETLTPS
     LDLIGKI
//

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