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PRDX_CHAMQ
ID   PRDX_CHAMQ              Reviewed;         195 AA.
AC   A0A2Z5VKM8; C0HLQ9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=2-cysteine peroxiredoxin, chloroplastic {ECO:0000305};
DE            Short=2-Cys Prx {ECO:0000305};
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:Q96291};
DE   AltName: Full=Thiol-specific antioxidant protein {ECO:0000305};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
OS   Chattonella marina var. antiqua (Red tide flagellate) (Chattonella
OS   antiqua).
OG   Plastid; Chloroplast {ECO:0000312|EMBL:BBB37582.1}.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Raphidophyceae; Chattonellales;
OC   Chattonellaceae; Chattonella.
OX   NCBI_TaxID=859642;
RN   [1] {ECO:0000312|EMBL:BBB37582.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=NIES-1 {ECO:0000312|EMBL:BBB37582.1};
RA   Mukai K., Teramoto A., Qiu X., Shimasaki Y., Kato-Unoki Y., Lee J.M.,
RA   Mizoguchi N., Khanam M.R.M., Satone H., Tatsuke T., Kusakabe T., Oshima Y.;
RT   "Gene structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful
RT   algal bloom species Chattonella marina and its gene transcription under
RT   different light intensities.";
RL   Eur. J. Phycol. 53:29-38(2018).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
RC   STRAIN=NIES-1 {ECO:0000303|PubMed:23291769};
RX   PubMed=23291769; DOI=10.1271/bbb.120543;
RA   Qiu X., Shimasaki Y., Tsuyama M., Yamada T., Kuwahara R., Kawaguchi M.,
RA   Honda M., Gunjikake H., Tasmin R., Shimizu M., Sato Y., Kato-Unoki Y.,
RA   Nakashima T., Matsubara T., Yamasaki Y., Ichinose H., Wariishi H.,
RA   Honjo T., Oshima Y.;
RT   "Growth-phase dependent variation in photosynthetic activity and cellular
RT   protein expression profile in the harmful raphidophyte Chattonella
RT   antiqua.";
RL   Biosci. Biotechnol. Biochem. 77:46-52(2013).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=NIES-1 {ECO:0000303|Ref.3};
RX   DOI=10.1016/j.jembe.2020.151361;
RA   Qiu X., Mukai K., Shimasaki Y., Wu M., Chen C., Lu Y., Ichinose H.,
RA   Nakashima T., Kato-Unoki Y., Oshima Y.;
RT   "Diurnal variations in expression of photosynthesis-related proteins in the
RT   harmful Raphidophyceae Chattonella marina var. antiqua.";
RL   J. Exp. Mar. Biol. Ecol. 527:0-0(2020).
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:0000250|UniProtKB:Q96291}.
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:Q96291};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC       {ECO:0000250|UniProtKB:Q06830}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:Q96291}.
CC   -!- INDUCTION: Up-regulated by high-intensity light and H2O2 (Ref.1). Down-
CC       regulated in the late stationary growth phase as compared to the early
CC       stationary and exponential growth phases (PubMed:23291769).
CC       {ECO:0000269|PubMed:23291769, ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; LC337661; BBB37582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z5VKM8; -.
DR   SMR; A0A2Z5VKM8; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   Chloroplast; Direct protein sequencing; Disulfide bond; Oxidoreductase;
KW   Plastid.
FT   CHAIN           1..195
FT                   /note="2-cysteine peroxiredoxin, chloroplastic"
FT                   /id="PRO_0000450269"
FT   DOMAIN          3..161
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        49
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000305"
FT   DISULFID        49
FT                   /note="Interchain (with C-173); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   DISULFID        170
FT                   /note="Interchain (with C-52); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
SQ   SEQUENCE   195 AA;  22013 MW;  CE6EA835BBFF5FDD CRC64;
     MSIRVGQKAP DFTATAVFDQ EFGTIRLSDY LDKRYVVLFF YPLDFTFVCP TEITAFSDRF
     KEFKELSTEV LGVSVDSEFS HLAWTQIDRK SGGLGELEYP LVSDLKKEIS SSYNVLTEDG
     VALRALFIID KEGIIQHSTV NNLSFGRNVD EALRTLQAIQ YSQENPDEVC PVNWKPGSKT
     MKPDPVGSKV YFEAI
 
 
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