ID   TDXH_HYPBU              Reviewed;         232 AA.
AC   A2BJD9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
DE            EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00401};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00401};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
GN   OrderedLocusNames=Hbut_0228;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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:0000255|HAMAP-Rule:MF_00401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00401};
CC   -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC       structure. {ECO:0000255|HAMAP-Rule:MF_00401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00401}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00401}.
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DR   EMBL; CP000493; ABM80100.1; -; Genomic_DNA.
DR   RefSeq; WP_011821417.1; NC_008818.1.
DR   AlphaFoldDB; A2BJD9; -.
DR   SMR; A2BJD9; -.
DR   STRING; 415426.Hbut_0228; -.
DR   EnsemblBacteria; ABM80100; ABM80100; Hbut_0228.
DR   GeneID; 4782634; -.
DR   KEGG; hbu:Hbut_0228; -.
DR   eggNOG; arCOG00312; Archaea.
DR   HOGENOM; CLU_042529_4_4_2; -.
DR   OMA; FWYPKDF; -.
DR   OrthoDB; 98508at2157; -.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   CDD; cd03016; PRX_1cys; 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; IPR045020; PRX_1cys.
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;
KW   Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..232
FT                   /note="Peroxiredoxin"
FT                   /id="PRO_1000049617"
FT   DOMAIN          6..161
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT   ACT_SITE        48
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT   DISULFID        48
FT                   /note="Interchain (with C-209); in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT   DISULFID        203..209
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT   DISULFID        209
FT                   /note="Interchain (with C-48); in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
SQ   SEQUENCE   232 AA;  26470 MW;  BDD21A392793316F CRC64;
     MPLQAPSIGE KFPEIEVMTT HGKIKLPDHF RGKWFVLFSH PADFTPVCTT EFVAFAKRYE
     DFKKLNTELI GLSVDSTFSH IKWAEWIKEK LGVEIPFPII ADPTGEVAKK LGLLHAQSST
     ATVRAVFVVD DKGVVRAILY YPQEVGRNID EILRLIESLQ ISDKYGRAIP ANWPNNELIG
     DNLIVPPAAT VQEAEERLKK FKCFDWWFCY EDKATAEEKE LARKFLKRVA NC