TPX_AQUAE
ID TPX_AQUAE Reviewed; 169 AA.
AC O66780;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00269};
GN Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269}; OrderedLocusNames=aq_488;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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_00269}.
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_00269};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269}.
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. In this atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000255|HAMAP-Rule:MF_00269}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00269}.
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DR EMBL; AE000657; AAC06736.1; -; Genomic_DNA.
DR PIR; H70343; H70343.
DR RefSeq; NP_213340.1; NC_000918.1.
DR RefSeq; WP_010880278.1; NC_000918.1.
DR PDB; 2YZH; X-ray; 1.85 A; A/B/C/D=1-169.
DR PDBsum; 2YZH; -.
DR AlphaFoldDB; O66780; -.
DR SMR; O66780; -.
DR STRING; 224324.aq_488; -.
DR EnsemblBacteria; AAC06736; AAC06736; aq_488.
DR KEGG; aae:aq_488; -.
DR PATRIC; fig|224324.8.peg.401; -.
DR eggNOG; COG2077; Bacteria.
DR HOGENOM; CLU_042529_12_2_0; -.
DR InParanoid; O66780; -.
DR OMA; ITQEPNY; -.
DR OrthoDB; 1738458at2; -.
DR EvolutionaryTrace; O66780; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR CDD; cd03014; PRX_Atyp2cys; 1.
DR HAMAP; MF_00269; Tpx; 1.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002065; TPX.
DR InterPro; IPR018219; Tpx_CS.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS01265; TPX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..169
FT /note="Thiol peroxidase"
FT /id="PRO_0000187868"
FT DOMAIN 19..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT ACT_SITE 61
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT DISULFID 61..95
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2YZH"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:2YZH"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:2YZH"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2YZH"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2YZH"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:2YZH"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2YZH"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:2YZH"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:2YZH"
SQ SEQUENCE 169 AA; 18573 MW; E815A4C9AFBF1C26 CRC64;
MARTVNLKGN PVTLVGPELK VGDRAPEAVV VTKDLQEKIV GGAKDVVQVI ITVPSLDTPV
CETETKKFNE IMAGMEGVDV TVVSMDLPFA QKRFCESFNI QNVTVASDFR YRDMEKYGVL
IGEGALKGIL ARAVFIIDKE GKVAYVQLVP EITEEPNYDE VVNKVKELI
