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Database: UniProt
Entry: A0A0L7M7S5_PLAF4
LinkDB: A0A0L7M7S5_PLAF4
Original site: A0A0L7M7S5_PLAF4 
ID   A0A0L7M7S5_PLAF4        Unreviewed;       216 AA.
AC   A0A0L7M7S5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN   ORFNames=PFDG_03866 {ECO:0000313|EMBL:KOB88907.1};
OS   Plasmodium falciparum (isolate Dd2).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=57267 {ECO:0000313|EMBL:KOB88907.1, ECO:0000313|Proteomes:UP000054282};
RN   [1] {ECO:0000313|Proteomes:UP000054282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA   Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "Annotation of Plasmodium falciparum Dd2.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Kodira C., Zeng Q., O'Leary S., Yandava C., Alvarado L., Wirth D.,
RA   Volkman S., Hartl D.;
RT   "The genome sequence of Plasmodium falciparum Dd2.";
RL   Submitted (SEP-2006) 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; GG701820; KOB88907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L7M7S5; -.
DR   SMR; A0A0L7M7S5; -.
DR   EnsemblProtists; KOB88907; KOB88907; PFDG_03866.
DR   VEuPathDB; PlasmoDB:PfDd2_120019700; -.
DR   OMA; NNFGVMR; -.
DR   Proteomes; UP000054282; Unassembled WGS sequence.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:RHEA.
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}; Peroxidase {ECO:0000256|PIRNR:PIRNR000239};
KW   Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054282}.
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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