ID   BAS1_HORVU              Reviewed;         210 AA.
AC   Q96468;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=BAS1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Gerbel; TISSUE=Leaf;
RX   PubMed=8790288; DOI=10.1007/bf00042228;
RA   Baier M., Dietz K.-J.;
RT   "Primary structure and expression of plant homologues of animal and fungal
RT   thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide
RT   reductases.";
RL   Plant Mol. Biol. 31:553-564(1996).
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   -!- TISSUE SPECIFICITY: Expressed in leaf blade, sheath, basiplast, stem
CC       and green spike. Maximal expression in young developing shoots segments
CC       where cell division and elongation take place. Not expressed in roots.
CC   -!- DEVELOPMENTAL STAGE: Maximal levels are seen in 4-day old seedlings and
CC       decline during aging of the seedling.
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; Z34917; CAA84396.1; -; mRNA.
DR   AlphaFoldDB; Q96468; -.
DR   SMR; Q96468; -.
DR   ExpressionAtlas; Q96468; 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   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   2: Evidence at transcript level;
KW   Antioxidant; Chloroplast; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Plastid; Redox-active center; Transit peptide.
FT   TRANSIT         <1..10
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           11..210
FT                   /note="2-Cys peroxiredoxin BAS1, chloroplastic"
FT                   /id="PRO_0000023785"
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;  23299 MW;  4DD488179D6BCAC9 CRC64;
     DARARSFVAR AAAEYDLPLV GNKAPDFAAE AVFDQEFINV KLSDYIGKKY VILFFYPLDF
     TFVCPTEITA FSDRHEEFEK INTEILGVSV DSVFSHLAWV QTERKSGGLG DLKYPLVSDV
     TKSISKSFGV LIPDQGIALR GLFIIDKEGV IQHSTINNLG IGRSVDETLR TLQALQYVKK
     PDEVCPAGWK PGEKSMKPDP KGSKEYFAAI