ID   A1STF6_PSYIN            Unreviewed;       158 AA.
AC   A1STF6;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 81.
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};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000256|ARBA:ARBA00042639};
GN   OrderedLocusNames=Ping_0929 {ECO:0000313|EMBL:ABM02771.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02771.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM02771.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM02771.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) 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=a hydroperoxide + [thioredoxin]-dithiol = an alcohol +
CC         [thioredoxin]-disulfide + 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:ARBA00049091};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00038489}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00691}.
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DR   EMBL; CP000510; ABM02771.1; -; Genomic_DNA.
DR   RefSeq; WP_011769334.1; NC_008709.1.
DR   AlphaFoldDB; A1STF6; -.
DR   STRING; 357804.Ping_0929; -.
DR   KEGG; pin:Ping_0929; -.
DR   eggNOG; COG1225; Bacteria.
DR   HOGENOM; CLU_042529_14_1_6; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000000639; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:TreeGrafter.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter.
DR   CDD; cd03017; PRX_BCP; 1.
DR   FunFam; 3.40.30.10:FF:000007; Thioredoxin-dependent thiol peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR050924; Peroxiredoxin_BCP/PrxQ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; NF006960; PRK09437.1; 1.
DR   PANTHER; PTHR42801:SF4; AHPC_TSA FAMILY PROTEIN; 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;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000639}.
FT   DOMAIN          4..157
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   158 AA;  17876 MW;  EEF6807F22445EB8 CRC64;
     MKRLVAGDKA PLFNLHDEQG KMIALADLTG KKVLVYFYPK AMTPGCINQA CGLRDVKTQL
     DDFNTLVFGI SPDPVKSLAN FVTKKELNFP LLSDQDHAVA EEFGVWGEKK FMGKVYDGIH
     RISFLINEQG IIEHVFDKFK TTDHQQVVLD YLKNKESI
//