ID A0A1W9GXI7_9PROT Unreviewed; 165 AA.
AC A0A1W9GXI7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Thiol peroxidase {ECO:0000256|HAMAP-Rule:MF_00269};
DE Short=Tpx {ECO:0000256|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_00269};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000256|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000256|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00269};
GN Name=tpx {ECO:0000256|HAMAP-Rule:MF_00269};
GN ORFNames=A4S08_05895 {ECO:0000313|EMBL:OQW39747.1};
OS Proteobacteria bacterium SG_bin4.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827381 {ECO:0000313|EMBL:OQW39747.1, ECO:0000313|Proteomes:UP000192864};
RN [1] {ECO:0000313|EMBL:OQW39747.1, ECO:0000313|Proteomes:UP000192864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin4 {ECO:0000313|EMBL:OQW39747.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00269};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00269}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00269}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQW39747.1}.
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DR EMBL; LWDH01000045; OQW39747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9GXI7; -.
DR STRING; 1827381.A4S08_05895; -.
DR Proteomes; UP000192864; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR CDD; cd03014; PRX_Atyp2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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 PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|HAMAP-Rule:MF_00269};
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00269};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00269};
KW Peroxidase {ECO:0000256|HAMAP-Rule:MF_00269, ECO:0000313|EMBL:OQW39747.1};
KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00269}.
FT DOMAIN 16..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 58
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
FT DISULFID 58..92
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
SQ SEQUENCE 165 AA; 17845 MW; 06189AF594FF325C CRC64;
MVTLKGKPIK IEGTFPKVGQ QAPAFSLVNR DLQDVTLANF AGKKKVLSIL PSLDTPVCAL
STRKFNQQAS NMDNTVVLII AADLPFAMSR FCDAEGLDKV VTLSTMRGAN FMKDYGVFIA
DSPFGGITAR AIIVLDEKDK IIHAELVPEI ADEPNYDAAM AALKQ
//
