BAS1A_ARATH
ID BAS1A_ARATH Reviewed; 266 AA.
AC Q96291; P92938; Q8L5U1; Q9S7Y0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=2-Cys peroxiredoxin BAS1, chloroplastic;
DE Short=2-Cys Prx A;
DE Short=2-Cys peroxiredoxin A;
DE EC=1.11.1.24 {ECO:0000269|PubMed:12084836};
DE AltName: Full=Thiol-specific antioxidant protein A;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin BAS1 {ECO:0000305};
DE Flags: Precursor;
GN Name=BAS1; OrderedLocusNames=At3g11630; ORFNames=F24K9.28, T19F11.3;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Baier M., Dietz K.-J.;
RT "2-Cys peroxiredoxin bas1 from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR96-031(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=9263459; DOI=10.1046/j.1365-313x.1997.12010179.x;
RA Baier M., Dietz K.-J.;
RT "The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast
RT protein: its expressional regulation, phylogenetic origin, and implications
RT for its specific physiological function in plants.";
RL Plant J. 12:179-190(1997).
RN [3]
RP SEQUENCE REVISION.
RA Baier M.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH CDSP32.
RX PubMed=12084836; DOI=10.1105/tpc.001644;
RA Broin M., Cuine S., Eymery F., Rey P.;
RT "The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin
RT involved in the protection of the photosynthetic apparatus against
RT oxidative damage.";
RL Plant Cell 14:1417-1432(2002).
RN [9]
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 [10]
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).
RN [11]
RP INTERACTION WITH ANTR-C.
RX PubMed=16884685; DOI=10.1016/j.bbrc.2006.07.088;
RA Moon J.C., Jang H.H., Chae H.B., Lee J.R., Lee S.Y., Jung Y.J., Shin M.R.,
RA Lim H.S., Chung W.S., Yun D.-J., Lee K.O., Lee S.Y.;
RT "The C-type Arabidopsis thioredoxin reductase ANTR-C acts as an electron
RT donor to 2-Cys peroxiredoxins in chloroplasts.";
RL Biochem. Biophys. Res. Commun. 348:478-484(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:0000269|PubMed:12084836}.
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:0000269|PubMed:12084836};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity).
CC Interacts with the plastidial thioredoxin CDSP32 (PubMed:12084836).
CC Interacts with the plastidial NADPH-dependent thioredoxin reductase
CC ANTR-C (PubMed:16884685). {ECO:0000250|UniProtKB:Q06830,
CC ECO:0000269|PubMed:12084836, ECO:0000269|PubMed:16884685}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9263459}.
CC -!- INDUCTION: Down-regulated under highly reduced cellular thiol pool
CC conditions. Down-regulated by ascorbate. Slightly induced by oxidative
CC stress. {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:0000305|PubMed:12084836}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X94218; CAA63909.1; -; mRNA.
DR EMBL; Y10478; CAA71503.1; -; mRNA.
DR EMBL; X97910; CAA66484.2; -; Genomic_DNA.
DR EMBL; AC008153; AAG51430.1; -; Genomic_DNA.
DR EMBL; AC009918; AAF02131.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75077.1; -; Genomic_DNA.
DR EMBL; AF324996; AAG40348.1; -; mRNA.
DR EMBL; AF419578; AAL31910.1; -; mRNA.
DR EMBL; AY079107; AAL84991.1; -; mRNA.
DR EMBL; AY086974; AAM64537.1; -; mRNA.
DR RefSeq; NP_187769.1; NM_111995.3.
DR PDB; 5ZTE; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=73-266.
DR PDBsum; 5ZTE; -.
DR AlphaFoldDB; Q96291; -.
DR SMR; Q96291; -.
DR BioGRID; 5669; 131.
DR IntAct; Q96291; 8.
DR MINT; Q96291; -.
DR STRING; 3702.AT3G11630.1; -.
DR PeroxiBase; 4358; At2CysPrx01.
DR iPTMnet; Q96291; -.
DR MetOSite; Q96291; -.
DR PaxDb; Q96291; -.
DR PRIDE; Q96291; -.
DR ProteomicsDB; 241127; -.
DR EnsemblPlants; AT3G11630.1; AT3G11630.1; AT3G11630.
DR GeneID; 820335; -.
DR Gramene; AT3G11630.1; AT3G11630.1; AT3G11630.
DR KEGG; ath:AT3G11630; -.
DR Araport; AT3G11630; -.
DR TAIR; locus:2080707; AT3G11630.
DR eggNOG; KOG0852; Eukaryota.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; Q96291; -.
DR OMA; EDSESCY; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; Q96291; -.
DR BioCyc; ARA:AT3G11630-MON; -.
DR PRO; PR:Q96291; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96291; baseline and differential.
DR Genevisible; Q96291; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:TAIR.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR InterPro; IPR000866; AhpC/TSA.
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 SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Chloroplast; Disulfide bond; Oxidoreductase;
KW Peroxidase; Plastid; Redox-active center; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 66..266
FT /note="2-Cys peroxiredoxin BAS1, chloroplastic"
FT /id="PRO_0000023784"
FT DOMAIN 73..232
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 119
FT /note="Interchain (with C-241); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 241
FT /note="Interchain (with C-119); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CONFLICT 83
FT /note="E -> K (in Ref. 1; CAA63909/CAA71503)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="I -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Missing (in Ref. 1; CAA66484)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..175
FT /note="DV -> YF (in Ref. 7; AAM64537)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="I -> IGI (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="R -> Q (in Ref. 7; AAM64537)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..235
FT /note="IQE -> TG (in Ref. 1; CAA63909/CAA71503)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="P -> S (in Ref. 1; CAA63909/CAA71503)"
FT /evidence="ECO:0000305"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5ZTE"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5ZTE"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:5ZTE"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:5ZTE"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5ZTE"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:5ZTE"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:5ZTE"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:5ZTE"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:5ZTE"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:5ZTE"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:5ZTE"
SQ SEQUENCE 266 AA; 29092 MW; 2CEB476A1A8694AD CRC64;
MASVASSTTL ISSPSSRVFP AKSSLSSPSV SFLRTLSSPS ASASLRSGFA RRSSLSSTSR
RSFAVKAQAD DLPLVGNKAP DFEAEAVFDQ EFIKVKLSDY IGKKYVILFF YPLDFTFVCP
TEITAFSDRH SEFEKLNTEV LGVSVDSVFS HLAWVQTDRK SGGLGDLNYP LISDVTKSIS
KSFGVLIHDQ GIALRGLFII DKEGVIQHST INNLGIGRSV DETMRTLQAL QYIQENPDEV
CPAGWKPGEK SMKPDPKLSK EYFSAI
