TDXH_THEP1
ID TDXH_THEP1 Reviewed; 215 AA.
AC A5IIX7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Tpet_0121;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000702; ABQ46150.1; -; Genomic_DNA.
DR RefSeq; WP_011942821.1; NC_009486.1.
DR AlphaFoldDB; A5IIX7; -.
DR SMR; A5IIX7; -.
DR STRING; 390874.Tpet_0121; -.
DR PRIDE; A5IIX7; -.
DR EnsemblBacteria; ABQ46150; ABQ46150; Tpet_0121.
DR KEGG; tpt:Tpet_0121; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_4_4_0; -.
DR OMA; MIDYQDT; -.
DR Proteomes; UP000006558; 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.
FT CHAIN 1..215
FT /note="Peroxiredoxin"
FT /id="PRO_1000049622"
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-211); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 205..211
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 211
FT /note="Interchain (with C-48); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
SQ SEQUENCE 215 AA; 24766 MW; 91B01EFAFCF2E422 CRC64;
MEGRIPLIGE EFPRLEVKTT HGKKILPDDF RGKWFVLFSH PADFTPVCTT EFVAFQKRYD
EFKKLNTELI GLSIDQVFSH IKWIEWIKEK LGVEIEFPVI ADDLGEVSRR LGLIHPSKGT
NTVRAVFIVD PNGIIRAIVY YPQEVGRNID EILRAVRALQ TSDEKGVAIP ANWPSNELIN
DSVIVPPASS VEEARERLES KDFECYDWWF CYKKV
