(data stored in SCRATCH zone)

SWISSPROT: D6XX72_BACIE

ID   D6XX72_BACIE            Unreviewed;       187 AA.
AC   D6XX72;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
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=Bsel_0389 {ECO:0000313|EMBL:ADH97929.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97929.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97929.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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}.
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; CP001791; ADH97929.1; -; Genomic_DNA.
DR   RefSeq; WP_013171358.1; NC_014219.1.
DR   STRING; 439292.Bsel_0389; -.
DR   EnsemblBacteria; ADH97929; ADH97929; Bsel_0389.
DR   KEGG; bse:Bsel_0389; -.
DR   eggNOG; ENOG4105D3R; Bacteria.
DR   eggNOG; COG0450; LUCA.
DR   HOGENOM; HOG000022343; -.
DR   KO; K03386; -.
DR   OMA; WYPKDFT; -.
DR   OrthoDB; 892697at2; -.
DR   BioCyc; BSEL439292:G1GLR-419-MONOMER; -.
DR   Proteomes; UP000000271; 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; D6XX72.
DR   SWISS-2DPAGE; D6XX72.
KW   Antioxidant {ECO:0000256|RuleBase:RU366004};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|RuleBase:RU366004};
KW   Disulfide bond {ECO:0000256|RuleBase:RU366004};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366004,
KW   ECO:0000313|EMBL:ADH97929.1};
KW   Peroxidase {ECO:0000256|RuleBase:RU366004,
KW   ECO:0000313|EMBL:ADH97929.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU366004};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
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;  20679 MW;  CC06F703A5AB45B3 CRC64;
     MSIIGTEVQP FTAQAYKNGD FVEVTEENFK GQWTILCFYP ADFTFVCPTE LEDLQNEYET
     LKNLGVEVYS ASTDTHFTHK GWHDSSETIG KIEYGMIGDP SQTLSRQFDV LNEESGLADR
     GTFIIDPDGV VQAAEINAEG IGRDASTLVN KIKAAQYVRN NPGEVCPAKW EEGDETLTPS
     LDLVGKI
//

If you have problems or comments...

PBIL Back to PBIL home page