ID   BAS1_SPIOL              Reviewed;         265 AA.
AC   O24364;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=2-Cys peroxiredoxin BAS1, chloroplastic;
DE            EC=1.11.1.15;
DE   AltName: Full=Thiol-specific antioxidant protein;
DE   Flags: Precursor;
GN   Name=BAS1;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Amaranthaceae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   MEDLINE=96382424; PubMed=8790288; DOI=10.1007/BF00042228;
RA   Baier M., Dietz K.-J.;
RT   "Primary structure and expression of plant homologues of animal and
RT   fungal thioredoxin-dependent peroxide reductases and bacterial alkyl
RT   hydroperoxide reductases.";
RL   Plant Mol. Biol. 31:553-564(1996).
CC   -!- FUNCTION: May be an antioxidant enzyme particularly in the
CC       developing shoot and photosynthesizing leaf.
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
CC   -!- PTM: The Cys-119-SH group is the primary site of oxidation by
CC       H(2)O(2), and the oxidized Cys-119 (probably Cys-SOH) rapidly
CC       reacts with Cys-240-SH of the other subunit to form an
CC       intermolecular disulfide. This disulfide might subsequently be
CC       reduced by thioredoxin (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; X94219; CAA63910.1; -; mRNA.
DR   PIR; T09211; T09211.
DR   HSSP; P32119; 1QMV.
DR   SMR; O24364; 75-263.
DR   IntAct; O24364; 1.
DR   PeroxiBase; 4408; So2CysPrx.
DR   BRENDA; 1.11.1.15; 286.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000866; Alkyl_hydroperoxide_Rdtase.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 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     65       Chloroplast (By similarity).
FT   CHAIN        66    265       2-Cys peroxiredoxin BAS1, chloroplastic.
FT                                /FTId=PRO_0000023786.
FT   DOMAIN       73    232       Thioredoxin.
FT   ACT_SITE    119    119       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   DISULFID    119    119       Interchain (with C-240); in linked form
FT                                (By similarity).
FT   DISULFID    240    240       Interchain (with C-119); in linked form
FT                                (By similarity).
SQ   SEQUENCE   265 AA;  28896 MW;  11F479093C2F573B CRC64;
     MACVASSTTL ISSPSSRVFP AKSSLSSPSV SFLRTLSSPS ASASLRSGFA RRSSLSSTSR
     RSFAVKAQAD DLPLVGNKAP DFEAEAVFDQ EFIKVKLSDY IGKKYVILFF YPLDFTFVCP
     TEITAFSDRH SEFEKLNTEV LGVSVDSVFS HLAWVQTDRK SGGLGDLNYP LISDVTKSIS
     KSFGVLIHDQ GIALRGLFII DKEGVIQHST INNLGIGRSV DETMRTLQAL QYTGNPDEVC
     PAGWKPGEKS MKPDPKLSKE YFSAI
//