ID A0A0S8JFI7_9BACT Unreviewed; 171 AA.
AC A0A0S8JFI7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AMJ85_08895 {ECO:0000313|EMBL:KPL08098.1};
OS candidate division BRC1 bacterium SM23_51.
OC Bacteria; Candidatus Sumerlaeota.
OX NCBI_TaxID=1703761 {ECO:0000313|EMBL:KPL08098.1, ECO:0000313|Proteomes:UP000051549};
RN [1] {ECO:0000313|EMBL:KPL08098.1, ECO:0000313|Proteomes:UP000051549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_51 {ECO:0000313|EMBL:KPL08098.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00269}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KPL08098.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJUL01000196; KPL08098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8JFI7; -.
DR PATRIC; fig|1703761.3.peg.1900; -.
DR Proteomes; UP000051549; 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 InterPro; IPR018219; Tpx_CS.
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.
DR PROSITE; PS01265; TPX; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW Rule:MF_00269}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00269};
KW Peroxidase {ECO:0000256|HAMAP-Rule:MF_00269};
KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00269}.
FT DOMAIN 22..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 64
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
SQ SEQUENCE 171 AA; 18750 MW; 35D183E7AC5F63A7 CRC64;
MEERTGIVTM RGNPLILVGS EVKVGDTAPD FTTLDNNLSP VAFSSFLGRV CIISSVPSLD
TPVCDRETRR FNEEAARLDP NLVILTISMD LPFAQKRWCG AAGVTRVQTL SDHRDASFGT
AYGVLIKELR LLARAVLVVD ADGIIRYVQI VNEVTEEPDY EAILTAVRTL P
//
