TPX_STRA3
ID TPX_STRA3 Reviewed; 164 AA.
AC Q8E536;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00269};
GN Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269}; OrderedLocusNames=gbs1198;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00269};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00269}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00269}.
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DR EMBL; AL766849; CAD46857.1; -; Genomic_DNA.
DR RefSeq; WP_000206547.1; NC_004368.1.
DR AlphaFoldDB; Q8E536; -.
DR SMR; Q8E536; -.
DR STRING; 211110.gbs1198; -.
DR EnsemblBacteria; CAD46857; CAD46857; CAD46857.
DR KEGG; san:gbs1198; -.
DR eggNOG; COG2077; Bacteria.
DR HOGENOM; CLU_042529_12_0_9; -.
DR OMA; ITQEPNY; -.
DR Proteomes; UP000000823; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR CDD; cd03014; PRX_Atyp2cys; 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 Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS01265; TPX; 1.
PE 3: Inferred from homology;
KW Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center.
FT CHAIN 1..164
FT /note="Thiol peroxidase"
FT /id="PRO_0000187908"
FT DOMAIN 16..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT ACT_SITE 58
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT DISULFID 58..92
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
SQ SEQUENCE 164 AA; 18388 MW; 5A5A1406071CA2CC CRC64;
MTTFLGNSVT FTGKQLQVGD IAKDFLLIAT DLSQKSLKDF EGKKKVISVV PSIDTGICSK
QTRTFNEELS ELDNTVVITV SMDLPFAQKR WCSAEGLDNV ILLSDFYDHS FGQDYALLMN
EWHLLTRAVL ILDEHNKVTY TEYVDNVNSD VDYEAAINAA KILP