TDXH_AQUAE
ID TDXH_AQUAE Reviewed; 222 AA.
AC O67024;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=aq_858;
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_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; AE000657; AAC06986.1; -; Genomic_DNA.
DR PIR; E70374; E70374.
DR RefSeq; NP_213585.1; NC_000918.1.
DR RefSeq; WP_010880523.1; NC_000918.1.
DR PDB; 5OVQ; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-222.
DR PDBsum; 5OVQ; -.
DR AlphaFoldDB; O67024; -.
DR SMR; O67024; -.
DR STRING; 224324.aq_858; -.
DR PRIDE; O67024; -.
DR EnsemblBacteria; AAC06986; AAC06986; aq_858.
DR KEGG; aae:aq_858; -.
DR PATRIC; fig|224324.8.peg.673; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_4_4_0; -.
DR InParanoid; O67024; -.
DR OMA; MIDYQDT; -.
DR OrthoDB; 892697at2; -.
DR Proteomes; UP000000798; 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; Disulfide bond; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..222
FT /note="Peroxiredoxin"
FT /id="PRO_0000135175"
FT DOMAIN 7..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 49
FT /note="Interchain (with C-218); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 212..218
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 218
FT /note="Interchain (with C-49); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:5OVQ"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:5OVQ"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:5OVQ"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:5OVQ"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:5OVQ"
SQ SEQUENCE 222 AA; 25308 MW; 1CF61BFAE6B1B992 CRC64;
MEVVSLPRLG EPAPAFEAQT TFGPVKFPDD FKGQWVVLFS HPADFTPVCT TEFVAFAKNY
EEFKKRNVQL IGLSVDSNFS HIAWVMNIKE KFGIEIPFPI IADHNMEVAK KYGMIHPAQS
TTFTVRALFV IDDKGILRAM IYYPLTTGRN IREVIRLVDA LQTADREGVA TPADWVPEPQ
TWEFTEENTK VIVPPPTTYE DAVKRLQEGY ECADWYICKK KV
