(data stored in ACNUC10043 zone)

SWISSPROT: D1YW83_METPS

ID   D1YW83_METPS            Unreviewed;       218 AA.
AC   D1YW83;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE            EC=1.11.1.15 {ECO:0000256|HAMAP-Rule:MF_00401};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00401};
GN   OrderedLocusNames=MCP_0633 {ECO:0000313|EMBL:BAI60705.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60705.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC         alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.15;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00401};
CC   -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. Although the primary
CC       sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes,
CC       its catalytic properties resemble those of the typical 2-Cys Prxs and
CC       C(R) is provided by the other dimeric subunit to form an intersubunit
CC       disulfide. The disulfide is subsequently reduced by thioredoxin.
CC       {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00401}.
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DR   EMBL; AP011532; BAI60705.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0633; -.
DR   EnsemblBacteria; BAI60705; BAI60705; MCP_0633.
DR   KEGG; mpd:MCP_0633; -.
DR   PATRIC; fig|304371.9.peg.652; -.
DR   eggNOG; arCOG00312; Archaea.
DR   eggNOG; COG0450; LUCA.
DR   HOGENOM; HOG000022346; -.
DR   KO; K03386; -.
DR   OMA; EKVMILP; -.
DR   BioCyc; MPAL304371:GI7G-649-MONOMER; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   HAMAP; MF_00401; Peroxiredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR022915; Peroxiredoxin_TDXH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YW83.
DR   SWISS-2DPAGE; D1YW83.
KW   Antioxidant {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Peroxidase {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   DOMAIN          14..169
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        55
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401,
FT                   ECO:0000256|PIRSR:PIRSR000239-1"
FT   BINDING         132
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT   DISULFID        55
FT                   /note="Interchain (with Cys-214); in linked form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT   DISULFID        208..214
FT                   /note="Alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT   DISULFID        214
FT                   /note="Interchain (with Cys-55); in linked form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
SQ   SEQUENCE   218 AA;  24712 MW;  A83AF6586B03B3F0 CRC64;
     MHDEVSVISP QGILSIGMPA PDFEAVTTHG KIKLSQYKGK WVVLFSHPSD FTPVCTTEFI
     AFAERYEDFK KRNVEIIGLS IDSVYSHIAW ARSIQEKTGC RIPFPIIADL DMRVAKAFNM
     IHPAMSETSA VRAVFFIDPN RILRAMVYYP QTTGRNMDEL LRIVDSLQIV DKEKVATPAN
     WRPGDAVIVP APNTQEGAEK RLNEGYECMD WYLCKKKL
//

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