ID   BAS1_WHEAT              Reviewed;         210 AA.
AC   P80602;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=2-Cys peroxiredoxin BAS1, chloroplastic;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:Q96291};
DE   AltName: Full=Thiol-specific antioxidant protein;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin BAS1 {ECO:0000305};
DE   Flags: Precursor; Fragment;
GN   Name=TSA;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Norin 61; TISSUE=Seedling;
RA   Tsunoyama Y., Toyoshima Y.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 11-35.
RC   STRAIN=cv. Norin 61; TISSUE=Leaf;
RA   Tsunoyama Y., Takashi S., Toyoshima Y.;
RL   Submitted (MAY-1996) to UniProtKB.
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: 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}.
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DR   EMBL; AB000405; BAA19099.1; -; mRNA.
DR   PIR; T06318; T06318.
DR   AlphaFoldDB; P80602; -.
DR   SMR; P80602; -.
DR   STRING; 4565.Traes_2AL_C6F2FA817.1; -.
DR   PeroxiBase; 4382; Ta2CysPrx.
DR   PRIDE; P80602; -.
DR   eggNOG; KOG0852; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P80602; baseline and differential.
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.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; Chloroplast; Direct protein sequencing; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Plastid; Redox-active center;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         <1..10
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           11..210
FT                   /note="2-Cys peroxiredoxin BAS1, chloroplastic"
FT                   /id="PRO_0000023787"
FT   DOMAIN          18..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        64
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   DISULFID        64
FT                   /note="Interchain (with C-185); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   DISULFID        185
FT                   /note="Interchain (with C-64); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   NON_TER         1
SQ   SEQUENCE   210 AA;  23327 MW;  E2D488179D6937E6 CRC64;
     DARARSFVAR AAAEYDLPLV GNKAPDFAAE AVFDQEFINV KLSDYIGKKY VILFFYPLDF
     TFVCPTEITA FSDRHEEFEK INTEILGVSV DSVFSHLAWV QTERKSGGLG DLKYPLVSDV
     TKSISKSFGV LIPDQGIALR GLFIIDKEGV IQHSTINNLG IGRSVDETLR TLRALQYVKK
     PDEVCPAGWK PGEKSMKPDP KGSKEYFAAI