ID   A7MGH6_CROS8            Unreviewed;       168 AA.
AC   A7MGH6;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 112.
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   OrderedLocusNames=ESA_01655 {ECO:0000313|EMBL:ABU76909.1};
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU76909.1, ECO:0000313|Proteomes:UP000000260};
RN   [1] {ECO:0000313|EMBL:ABU76909.1, ECO:0000313|Proteomes:UP000000260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU76909.1,
RC   ECO:0000313|Proteomes:UP000000260};
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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=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, ECO:0000256|HAMAP-
CC         Rule:MF_00269};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00691}.
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DR   EMBL; CP000783; ABU76909.1; -; Genomic_DNA.
DR   RefSeq; WP_004387306.1; NC_009778.1.
DR   AlphaFoldDB; A7MGH6; -.
DR   GeneID; 45715455; -.
DR   GeneID; 56730480; -.
DR   KEGG; esa:ESA_01655; -.
DR   HOGENOM; CLU_042529_12_2_6; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-ARBA.
DR   CDD; cd03014; PRX_Atyp2cys; 1.
DR   FunFam; 3.40.30.10:FF:000056; Thiol peroxidase; 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   InterPro; IPR050455; Tpx_Peroxidase_subfamily.
DR   NCBIfam; NF001808; PRK00522.1; 1.
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};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_00269};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00269};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW   Rule:MF_00269};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW   Rule:MF_00269}; Reference proteome {ECO:0000313|Proteomes:UP000000260}.
FT   DOMAIN          19..168
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        61
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
FT   DISULFID        61..95
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
SQ   SEQUENCE   168 AA;  17865 MW;  719DB6EAD72C66D9 CRC64;
     MSQIVYFQGN PVSVVGQIPQ AGSKAAPFSL VAKDLSDVSL SQFAGKRKVL NIFPSIDTGV
     CAASVRKFNQ LATGMENTVV LCVSADLPFA QSRFCGAEGL SNVITLSTLR NPEFAKEYGV
     GIEEGALKGL TARAVLVLNE NDEIVFSELV NEITHEPNYD AALNALKA
//