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Database: UniProt
Entry: W7JRH9_PLAFO
LinkDB: W7JRH9_PLAFO
Original site: W7JRH9_PLAFO 
ID   W7JRH9_PLAFO            Unreviewed;       216 AA.
AC   W7JRH9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN   ORFNames=CK202_1898 {ECO:0000313|EMBL:PKC48475.1}, CYL21_4578
GN   {ECO:0000313|EMBL:KAF4327104.1}, PFNF54_03687
GN   {ECO:0000313|EMBL:EWC87563.1};
OS   Plasmodium falciparum (isolate NF54).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5843 {ECO:0000313|EMBL:EWC87563.1, ECO:0000313|Proteomes:UP000030673};
RN   [1] {ECO:0000313|EMBL:EWC87563.1, ECO:0000313|Proteomes:UP000030673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NF54 {ECO:0000313|EMBL:EWC87563.1,
RC   ECO:0000313|Proteomes:UP000030673};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium falciparum NF54.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PKC48475.1, ECO:0000313|Proteomes:UP000232684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NF54 {ECO:0000313|EMBL:PKC48475.1};
RA   Bryant J.M., Baumgarten S., Scheidig-Benatar C., Scherf A.;
RT   "Plasmodium falciparum NF54 genome assembly.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF4327104.1, ECO:0000313|Proteomes:UP000754359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NF54 {ECO:0000313|EMBL:KAF4327104.1};
RA   Baumgarten S., Treeck M., Scherf A.;
RT   "Genome assembly of Plasmodium falciparum NF54 DiCre.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. {ECO:0000256|PIRNR:PIRNR000239}.
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:0000256|ARBA:ARBA00000280};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796}.
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DR   EMBL; KE123842; EWC87563.1; -; Genomic_DNA.
DR   EMBL; QFXU01000022; KAF4327104.1; -; Genomic_DNA.
DR   EMBL; NYMT01000004; PKC48475.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7JRH9; -.
DR   SMR; W7JRH9; -.
DR   EnsemblProtists; EWC87563; EWC87563; PFNF54_03687.
DR   OMA; NNFGVMR; -.
DR   Proteomes; UP000030673; Unassembled WGS sequence.
DR   Proteomes; UP000232684; Unassembled WGS sequence.
DR   Proteomes; UP000754359; Unassembled WGS sequence.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   PANTHER; PTHR10681:SF164; THIOREDOXIN PEROXIDASE 1; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|PIRNR:PIRNR000239};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000239};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR000239, ECO:0000313|EMBL:KAF4327104.1};
KW   Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030673}.
FT   DOMAIN          20..179
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        67
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   216 AA;  24680 MW;  C73610CDD1015C1B CRC64;
     MFLKKLCRSN FFGNSRRSFS LVTKKAYNFT AQGLNKNNEI INVDLSSFIG QKYCCLLFYP
     LNYTFVCPTE IIEFNKHIKD FENKNVELLG ISVDSVYSHL AWKNMPIEKG GIGNVEFTLV
     SDINKDISKN YNVLYDNSFA LRGLFIIDKN GCVRHQTVND LPIGRNVQEV LRTIDSIIHV
     DTSGEVCPIN WKKGQKAFKP TTESLIDYMN NANKNV
//
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