ID   BAS1_PINST              Reviewed;          56 AA.
AC   P84729;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Putative 2-Cys peroxiredoxin BAS1;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:Q96291};
DE   AltName: Full=PS13;
DE   AltName: Full=Thiol-specific antioxidant protein;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin BAS1 {ECO:0000305};
DE   Flags: Fragments;
OS   Pinus strobus (Eastern white pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=3348;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|PubMed:16529377};
RX   PubMed=16529377; DOI=10.1094/mpmi-19-0150;
RA   Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L.,
RA   Witthuhn B.A., David A.J., Gillman J.H.;
RT   "Proteomic comparison of needles from blister rust-resistant and
RT   susceptible Pinus strobus seedlings reveals upregulation of putative
RT   disease resistance proteins.";
RL   Mol. Plant Microbe Interact. 19:150-160(2006).
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. May be an antioxidant enzyme particularly in
CC       the developing shoot and photosynthesizing leaf.
CC       {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   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.7,
CC       its MW is: 22.8 kDa. {ECO:0000269|PubMed:16529377}.
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:Q96291}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:16529377}.
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DR   AlphaFoldDB; P84729; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Antioxidant; Chloroplast; Direct protein sequencing; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Plastid; Redox-active center.
FT   CHAIN           <1..>56
FT                   /note="Putative 2-Cys peroxiredoxin BAS1"
FT                   /id="PRO_0000240611"
FT   NON_CONS        18..19
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        34..35
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        47..48
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         56
FT                   /evidence="ECO:0000303|PubMed:16529377"
SQ   SEQUENCE   56 AA;  5894 MW;  FCC2ECB15318133E CRC64;
     GLFIIDKEGV IQHSTINNEG VIQHSTINNL AIGRFGVLLA DQGLALRSIP NGPSAL