CR29_ENTHI
ID CR29_ENTHI Reviewed; 233 AA.
AC P19476;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Putative peroxiredoxin;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE AltName: Full=29 kDa cysteine-rich surface antigen;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8367659;
RA Bruchhaus I., Tannich E.;
RT "Analysis of the genomic sequence encoding the 29-kDa cysteine-rich protein
RT of Entamoeba histolytica.";
RL Trop. Med. Parasitol. 44:116-118(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-233.
RX PubMed=1730488; DOI=10.1128/iai.60.2.542-549.1992;
RA Reed S.L., Flores B.M., Batzer M.A., Stein M.A., Stroeher V.L.,
RA Carlton J.E., Diedrich D.L., Torian B.E.;
RT "Molecular and cellular characterization of the 29-kilodalton peripheral
RT membrane protein of Entamoeba histolytica: differentiation between
RT pathogenic and nonpathogenic isolates.";
RL Infect. Immun. 60:542-549(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-233.
RC STRAIN=H-302:NIH;
RX PubMed=2201027; DOI=10.1073/pnas.87.16.6358;
RA Torian B.E., Flores B.M., Stroeher V.L., Hagen F.S., Stamm W.E.;
RT "cDNA sequence analysis of a 29-kDa cysteine-rich surface antigen of
RT pathogenic Entamoeba histolytica.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6358-6362(1990).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=7682280; DOI=10.1111/j.1365-2958.1993.tb01166.x;
RA Flores B.M., Batzer M.A., Stein M.A., Petersen C., Diedrich D.L.,
RA Torian B.E.;
RT "Structural analysis and demonstration of the 29 kDa antigen of pathogenic
RT Entamoeba histolytica as the major accessible free thiol-containing surface
RT protein.";
RL Mol. Microbiol. 7:755-763(1993).
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:0000250|UniProtKB:Q06830}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q06830};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC {ECO:0000269|PubMed:7682280}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Extracellular side {ECO:0000269|PubMed:7682280}.
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 typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:Q06830}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X70996; CAA50324.1; -; Genomic_DNA.
DR EMBL; M75858; AAA29110.1; ALT_SEQ; mRNA.
DR EMBL; M35635; AAA29095.1; -; mRNA.
DR PIR; S67947; S67947.
DR AlphaFoldDB; P19476; -.
DR SMR; P19476; -.
DR STRING; 5759.rna_EHI_061980-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_261670; -.
DR VEuPathDB; AmoebaDB:EHI7A_131930; -.
DR VEuPathDB; AmoebaDB:EHI8A_147450; -.
DR VEuPathDB; AmoebaDB:EHI_061980; -.
DR VEuPathDB; AmoebaDB:KM1_154550; -.
DR VEuPathDB; AmoebaDB:KM1_197060; -.
DR eggNOG; KOG0852; Eukaryota.
DR OMA; CPLGWKP; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cell membrane; Disulfide bond; Membrane; Oxidoreductase;
KW Peroxidase; Redox-active center.
FT CHAIN 1..233
FT /note="Putative peroxiredoxin"
FT /id="PRO_0000135100"
FT DOMAIN 41..200
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 87
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 87
FT /note="Interchain (with C-208); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 208
FT /note="Interchain (with C-87); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CONFLICT 70
FT /note="R -> K (in Ref. 3; AAA29095)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="N -> D (in Ref. 2; AAA29110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 26253 MW; 3FFE70141692FF88 CRC64;
MSCNQQKECC KKECQEKECC KECCCPRIKA FKKFINTFEK AQIGKEAPEF KAPAYCPCGS
IKEIDINEYR GKYVVLLFYP LDWTFVCPTE MIGYSELAGQ LKEINCEVIG VSVDSVYCHQ
AWCEADKSKG GVGKLTFPLV SDIKRCISIK YGMLNVEAGI ARRGYVIIDD KGKVRYIQMN
DDGIGRSTEE TIRIVKAIQF SDEHGAVCPL NWKPGKDTIE PTPDGIKKYL TAH
