TPX_STRPN
ID TPX_STRPN Reviewed; 163 AA.
AC P0C2J8; P0A4M5; P72500; Q9R6P4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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}; Synonyms=psaD;
GN OrderedLocusNames=SP_1651;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK75730.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005672; AAK75730.1; ALT_INIT; Genomic_DNA.
DR PIR; A95192; A95192.
DR RefSeq; WP_000256028.1; NZ_AKVY01000001.1.
DR PDB; 1PSQ; X-ray; 2.30 A; A/B=1-163.
DR PDBsum; 1PSQ; -.
DR AlphaFoldDB; P0C2J8; -.
DR SMR; P0C2J8; -.
DR STRING; 170187.SP_1651; -.
DR EnsemblBacteria; AAK75730; AAK75730; SP_1651.
DR GeneID; 60233547; -.
DR GeneID; 66806727; -.
DR KEGG; spn:SP_1651; -.
DR eggNOG; COG2077; Bacteria.
DR OMA; ITQEPNY; -.
DR PhylomeDB; P0C2J8; -.
DR BioCyc; SPNE170187:G1FZB-1672-MON; -.
DR EvolutionaryTrace; P0C2J8; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center.
FT CHAIN 1..163
FT /note="Thiol peroxidase"
FT /id="PRO_0000187913"
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"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1PSQ"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1PSQ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1PSQ"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1PSQ"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1PSQ"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:1PSQ"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1PSQ"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1PSQ"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:1PSQ"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1PSQ"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1PSQ"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:1PSQ"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1PSQ"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1PSQ"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1PSQ"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:1PSQ"
SQ SEQUENCE 163 AA; 18019 MW; 4BFA6C755541997B CRC64;
MVTFLGNPVS FTGKQLQVGD KALDFSLTTT DLSKKSLADF DGKKKVLSVV PSIDTGICST
QTRRFNEELA GLDNTVVLTV SMDLPFAQKR WCGAEGLDNA IMLSDYFDHS FGRDYALLIN
EWHLLARAVF VLDTDNTIRY VEYVDNINSE PNFEAAIAAA KAL
