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Database: UniProt
Entry: A0A1G5FK72_9CLOT
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Original site: A0A1G5FK72_9CLOT 
ID   A0A1G5FK72_9CLOT        Unreviewed;       169 AA.
AC   A0A1G5FK72;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN03080606_01447 {ECO:0000313|EMBL:SCY39656.1};
OS   Alkaliphilus peptidifermentans DSM 18978.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=1120976 {ECO:0000313|EMBL:SCY39656.1, ECO:0000313|Proteomes:UP000198636};
RN   [1] {ECO:0000313|EMBL:SCY39656.1, ECO:0000313|Proteomes:UP000198636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18978 {ECO:0000313|EMBL:SCY39656.1,
RC   ECO:0000313|Proteomes:UP000198636};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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. {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}.
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DR   EMBL; FMUS01000007; SCY39656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5FK72; -.
DR   STRING; 1120976.SAMN03080606_01447; -.
DR   OrthoDB; 9781543at2; -.
DR   Proteomes; UP000198636; 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|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW   Rule:MF_00269}; Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00269};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00269};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW   Rule:MF_00269}; Redox-active center {ECO:0000256|HAMAP-Rule:MF_00269};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198636}.
FT   DOMAIN          22..169
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"
FT   DISULFID        64..98
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
SQ   SEQUENCE   169 AA;  18850 MW;  F1A0A4C2743FD9CD CRC64;
     MDKRKSVVTM KGNPVTLLGK EMMVGDIAPN FTAVTKDLKE FTLKDMEGKI KLISVVPSID
     TGVCDLQTMT FNEEAEKLNN TVVVTISMDL PFALNRYCAA KGLENAITLS DHREASFGLA
     YGFLIEELRL LARGVIVLDQ NNKVIYVEYV NEISQQPNYD KALETVKQL
//
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