TDXH_THEKO
ID TDXH_THEKO Reviewed; 216 AA.
AC Q5JF30;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=TK0537;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=12065581; DOI=10.1074/jbc.m202868200;
RA Rashid N., Imanaka H., Kanai T., Fukui T., Atomi H., Imanaka T.;
RT "A novel candidate for the true fructose-1,6-bisphosphatase in archaea.";
RL J. Biol. Chem. 277:30649-30655(2002).
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; AP006878; BAD84726.1; -; Genomic_DNA.
DR RefSeq; WP_011249492.1; NC_006624.1.
DR PDB; 6ITZ; X-ray; 2.96 A; A/B=1-216.
DR PDB; 6IU0; X-ray; 2.38 A; A/B=1-216.
DR PDBsum; 6ITZ; -.
DR PDBsum; 6IU0; -.
DR AlphaFoldDB; Q5JF30; -.
DR SMR; Q5JF30; -.
DR STRING; 69014.TK0537; -.
DR EnsemblBacteria; BAD84726; BAD84726; TK0537.
DR GeneID; 3233785; -.
DR KEGG; tko:TK0537; -.
DR PATRIC; fig|69014.16.peg.525; -.
DR eggNOG; arCOG00312; Archaea.
DR HOGENOM; CLU_042529_4_4_2; -.
DR InParanoid; Q5JF30; -.
DR OMA; FWYPKDF; -.
DR OrthoDB; 98508at2157; -.
DR PhylomeDB; Q5JF30; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..216
FT /note="Peroxiredoxin"
FT /id="PRO_0000135166"
FT DOMAIN 2..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 46
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-46); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6IU0"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:6IU0"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6IU0"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6IU0"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:6IU0"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6IU0"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6IU0"
SQ SEQUENCE 216 AA; 24646 MW; B4F7BDE7B8A1EEC1 CRC64;
MVVIGEKFPE VEVKTTHGVI KLPDYFAEQG KWFVLFSHPA DFTPVCTTEF YAMQKRVDQF
RELGVEPIGL SVDQVFSHIK WMEWIKENLG EEITFPVIAD DRGELADKLG MIPSGATITA
RAVFIVDDKG IIRAIVYYPA EVGRDWDEIL RLVKALKVSD EKGVALPHKW PNNELIGDKA
IVPPASTVDE VKQREEAKAK GEIECYDWWF CYKKLE
