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Database: UniProt
Entry: E8WL70_GEOS8
LinkDB: E8WL70_GEOS8
Original site: E8WL70_GEOS8 
ID   E8WL70_GEOS8            Unreviewed;       158 AA.
AC   E8WL70;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
GN   OrderedLocusNames=GM18_0161 {ECO:0000313|EMBL:ADW11650.1};
OS   Geobacter sp. (strain M18).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW11650.1, ECO:0000313|Proteomes:UP000001442};
RN   [1] {ECO:0000313|EMBL:ADW11650.1, ECO:0000313|Proteomes:UP000001442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18 {ECO:0000313|EMBL:ADW11650.1,
RC   ECO:0000313|Proteomes:UP000001442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA   Aklujkar M., Lovley D., Woyke T.;
RT   "Complete sequence of Geobacter sp. M18.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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 and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000256|ARBA:ARBA00003330}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000280};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00038489}.
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DR   EMBL; CP002479; ADW11650.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8WL70; -.
DR   STRING; 443143.GM18_0161; -.
DR   KEGG; geb:GM18_0161; -.
DR   eggNOG; COG1225; Bacteria.
DR   HOGENOM; CLU_042529_14_1_7; -.
DR   OMA; MNTHADR; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000001442; Chromosome.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd03017; PRX_BCP; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42801:SF4; AHPC/TSA FAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          2..156
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   158 AA;  17500 MW;  EFCDF94557C1EE76 CRC64;
     MFLEGQKAPD FKLQGSDGRE HTLKDYRGKI VVLFFYPRDN TPGCTAEAVG FAKLQPLFEQ
     LGAVLVGVSK DSLKSHDKFI ADFKLPFTLL SDPDASVMKT YGAFGEKVQY GKTTMGTIRS
     TVVISPEGTV IKHWPKVAKA SEHPDKVLDF FKMLAKGR
//
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