TPX_VIBC3
ID TPX_VIBC3 Reviewed; 164 AA.
AC A5F3A2; C3LYI9; P39167; Q9KTR6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=tagD;
GN OrderedLocusNames=VC0395_A0349, VC395_0840;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7523254; DOI=10.1016/0378-1119(94)90240-2;
RA Hughes K.J., Everiss K.D., Harkey C.W., Peterson K.M.;
RT "Identification of a Vibrio cholerae ToxR-activated gene (tagD) that is
RT physically linked to the toxin-coregulated pilus (tcp) gene cluster.";
RL Gene 148:97-100(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; U02375; AAA64918.1; -; Genomic_DNA.
DR EMBL; CP000627; ABQ20151.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP08855.1; -; Genomic_DNA.
DR RefSeq; WP_000218963.1; NZ_JAACZH010000023.1.
DR AlphaFoldDB; A5F3A2; -.
DR SMR; A5F3A2; -.
DR STRING; 345073.VC395_0840; -.
DR EnsemblBacteria; ABQ20151; ABQ20151; VC0395_A0349.
DR KEGG; vco:VC0395_A0349; -.
DR KEGG; vcr:VC395_0840; -.
DR PATRIC; fig|345073.21.peg.812; -.
DR eggNOG; COG2077; Bacteria.
DR HOGENOM; CLU_042529_12_2_6; -.
DR OMA; DICETTV; -.
DR Proteomes; UP000000249; Chromosome 2.
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_0000324779"
FT DOMAIN 17..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT ACT_SITE 59
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT DISULFID 59..93
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
SQ SEQUENCE 164 AA; 17924 MW; 128945C4D2DF48CA CRC64;
MTVTFQNNPV SISGSFPKVG DRLPSFTLCG ADLNDLNNED FKGKKIVMSI FPSIDTPVCS
KSVKVLQNAL MTRSDTVLLC VSADLPFAMS RFCTEHAVAN VTNASFFREP AFTERFGVNL
NEGALRGLAA RAVIVADEFG VITHSELVNE ITNEPDYDRI LMSL
