ID BAS1B_ARATH Reviewed; 273 AA.
AC Q9C5R8; Q9FED5; Q9FNH9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=2-Cys peroxiredoxin BAS1-like, chloroplastic;
DE Short=2-Cys Prx B;
DE Short=2-Cys peroxiredoxin B;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q96291};
DE AltName: Full=Thiol-specific antioxidant protein B;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin BAS1-like {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At5g06290; ORFNames=MHF15.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INDUCTION.
RX PubMed=12529539; DOI=10.1104/pp.010017;
RA Horling F., Lamkemeyer P., Koenig J., Finkemeier I., Kandlbinder A.,
RA Baier M., Dietz K.-J.;
RT "Divergent light-, ascorbate-, and oxidative stress-dependent regulation of
RT expression of the peroxiredoxin gene family in Arabidopsis.";
RL Plant Physiol. 131:317-325(2003).
RN [5]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=15890615; DOI=10.1016/j.freeradbiomed.2004.07.037;
RA Rouhier N., Jacquot J.-P.;
RT "The plant multigenic family of thiol peroxidases.";
RL Free Radic. Biol. Med. 38:1413-1421(2005).
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 (By similarity).
CC Interacts with the plastidial thioredoxin CDSP32. Interacts with the
CC plastidial NADPH-dependent thioredoxin reductase ANTR-C (By
CC similarity). {ECO:0000250|UniProtKB:Q06830,
CC ECO:0000250|UniProtKB:Q96291}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q96291}.
CC -!- INDUCTION: Down-regulated by ascorbate. {ECO:0000269|PubMed:12529539}.
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 CDSP32. {ECO:0000250|UniProtKB:Q96291}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG40040.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB08951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB006700; BAB08951.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED90999.1; -; Genomic_DNA.
DR EMBL; AF324689; AAG40040.2; ALT_INIT; mRNA.
DR EMBL; AF326871; AAG41453.1; -; mRNA.
DR EMBL; AF339693; AAK00375.1; -; mRNA.
DR EMBL; AY054621; AAK96812.1; -; mRNA.
DR EMBL; AY081503; AAM10065.1; -; mRNA.
DR RefSeq; NP_568166.1; NM_120712.4.
DR AlphaFoldDB; Q9C5R8; -.
DR SMR; Q9C5R8; -.
DR BioGRID; 15796; 23.
DR IntAct; Q9C5R8; 3.
DR MINT; Q9C5R8; -.
DR STRING; 3702.Q9C5R8; -.
DR PeroxiBase; 4361; At2CysPrx02.
DR iPTMnet; Q9C5R8; -.
DR PaxDb; 3702-AT5G06290-1; -.
DR ProteomicsDB; 240715; -.
DR EnsemblPlants; AT5G06290.1; AT5G06290.1; AT5G06290.
DR GeneID; 830517; -.
DR Gramene; AT5G06290.1; AT5G06290.1; AT5G06290.
DR KEGG; ath:AT5G06290; -.
DR Araport; AT5G06290; -.
DR TAIR; AT5G06290; 2-CYS PRX B.
DR eggNOG; KOG0852; Eukaryota.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; Q9C5R8; -.
DR OMA; FWYPKDF; -.
DR OrthoDB; 47465at2759; -.
DR BioCyc; ARA:AT5G06290-MONOMER; -.
DR PRO; PR:Q9C5R8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5R8; baseline and differential.
DR Genevisible; Q9C5R8; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:TAIR.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF175; 2-CYS PEROXIREDOXIN BAS1-LIKE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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; Reference proteome; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 73..273
FT /note="2-Cys peroxiredoxin BAS1-like, chloroplastic"
FT /id="PRO_0000284083"
FT DOMAIN 80..239
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 126
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 126
FT /note="Interchain (with C-248); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 248
FT /note="Interchain (with C-126); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CONFLICT 217
FT /note="T -> P (in Ref. 3; AAG40040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29780 MW; 33CB87338DADEB1B CRC64;
MSMASIASSS STTLLSSSRV LLPSKSSLLS PTVSFPRIIP SSSASSSSLC SGFSSLGSLT
TNRSASRRNF AVKAQADDLP LVGNKAPDFE AEAVFDQEFI KVKLSEYIGK KYVILFFYPL
DFTFVCPTEI TAFSDRYEEF EKLNTEVLGV SVDSVFSHLA WVQTDRKSGG LGDLNYPLVS
DITKSISKSF GVLIPDQGIA LRGLFIIDKE GVIQHSTINN LGIGRSVDET MRTLQALQYV
QENPDEVCPA GWKPGEKSMK PDPKLSKEYF SAI
//
