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2-Cys peroxiredoxin BAS1, chloroplastic (2-Cys Prx A) (2-Cys peroxiredoxin A) (EC 1.11.1.15) (Thiol-specific antioxidant protein A)

 BAS1A_ARATH             Reviewed;         266 AA.
Q96291; P92938; Q8L5U1; Q9S7Y0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 2.
23-MAY-2018, entry version 149.
RecName: Full=2-Cys peroxiredoxin BAS1, chloroplastic;
Short=2-Cys Prx A;
Short=2-Cys peroxiredoxin A;
EC=1.11.1.15 {ECO:0000269|PubMed:12084836};
AltName: Full=Thiol-specific antioxidant protein A;
Flags: Precursor;
Name=BAS1; OrderedLocusNames=At3g11630; ORFNames=F24K9.28, T19F11.3;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Baier M., Dietz K.-J.;
"2-Cys peroxiredoxin bas1 from Arabidopsis thaliana.";
(er) Plant Gene Register PGR96-031(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=9263459; DOI=10.1046/j.1365-313X.1997.12010179.x;
Baier M., Dietz K.-J.;
"The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast
protein: its expressional regulation, phylogenetic origin, and
implications for its specific physiological function in plants.";
Plant J. 12:179-190(1997).
[3]
SEQUENCE REVISION.
Baier M.;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH CDSP32.
PubMed=12084836; DOI=10.1105/tpc.001644;
Broin M., Cuine S., Eymery F., Rey P.;
"The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin
involved in the protection of the photosynthetic apparatus against
oxidative damage.";
Plant Cell 14:1417-1432(2002).
[9]
INDUCTION.
PubMed=12529539; DOI=10.1104/pp.010017;
Horling F., Lamkemeyer P., Koenig J., Finkemeier I., Kandlbinder A.,
Baier M., Dietz K.-J.;
"Divergent light-, ascorbate-, and oxidative stress-dependent
regulation of expression of the peroxiredoxin gene family in
Arabidopsis.";
Plant Physiol. 131:317-325(2003).
[10]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
PubMed=15890615; DOI=10.1016/j.freeradbiomed.2004.07.037;
Rouhier N., Jacquot J.-P.;
"The plant multigenic family of thiol peroxidases.";
Free Radic. Biol. Med. 38:1413-1421(2005).
[11]
INTERACTION WITH ANTR-C.
PubMed=16884685; DOI=10.1016/j.bbrc.2006.07.088;
Moon J.C., Jang H.H., Chae H.B., Lee J.R., Lee S.Y., Jung Y.J.,
Shin M.R., Lim H.S., Chung W.S., Yun D.-J., Lee K.O., Lee S.Y.;
"The C-type Arabidopsis thioredoxin reductase ANTR-C acts as an
electron donor to 2-Cys peroxiredoxins in chloroplasts.";
Biochem. Biophys. Res. Commun. 348:478-484(2006).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides. May be an antioxidant
enzyme particularly in the developing shoot and photosynthesizing
leaf. {ECO:0000269|PubMed:12084836}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:12084836}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By
similarity). Interacts with the plastidial thioredoxin CDSP32
(PubMed:12084836). Interacts with the plastidial NADPH-dependent
thioredoxin reductase ANTR-C (PubMed:16884685).
{ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:12084836,
ECO:0000269|PubMed:16884685}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:9263459}.
-!- INDUCTION: Down-regulated under highly reduced cellular thiol pool
conditions. Down-regulated by ascorbate. Slightly induced by
oxidative stress. {ECO:0000269|PubMed:12529539}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin CDSP32.
{ECO:0000305|PubMed:12084836}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X94218; CAA63909.1; -; mRNA.
EMBL; Y10478; CAA71503.1; -; mRNA.
EMBL; X97910; CAA66484.2; -; Genomic_DNA.
EMBL; AC008153; AAG51430.1; -; Genomic_DNA.
EMBL; AC009918; AAF02131.1; -; Genomic_DNA.
EMBL; CP002686; AEE75077.1; -; Genomic_DNA.
EMBL; AF324996; AAG40348.1; -; mRNA.
EMBL; AF419578; AAL31910.1; -; mRNA.
EMBL; AY079107; AAL84991.1; -; mRNA.
EMBL; AY086974; AAM64537.1; -; mRNA.
RefSeq; NP_187769.1; NM_111995.3.
UniGene; At.22950; -.
UniGene; At.68687; -.
ProteinModelPortal; Q96291; -.
SMR; Q96291; -.
BioGrid; 5669; 10.
IntAct; Q96291; 7.
MINT; Q96291; -.
STRING; 3702.AT3G11630.1; -.
PeroxiBase; 4358; At2CysPrx01.
iPTMnet; Q96291; -.
PaxDb; Q96291; -.
PRIDE; Q96291; -.
EnsemblPlants; AT3G11630.1; AT3G11630.1; AT3G11630.
GeneID; 820335; -.
Gramene; AT3G11630.1; AT3G11630.1; AT3G11630.
KEGG; ath:AT3G11630; -.
Araport; AT3G11630; -.
TAIR; locus:2080707; AT3G11630.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
HOGENOM; HOG000022343; -.
InParanoid; Q96291; -.
KO; K03386; -.
OMA; MVYYPMT; -.
OrthoDB; EOG09360MKG; -.
PhylomeDB; Q96291; -.
BioCyc; ARA:AT3G11630-MONOMER; -.
BRENDA; 1.11.1.15; 399.
Reactome; R-ATH-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q96291; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q96291; baseline and differential.
Genevisible; Q96291; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0010319; C:stromule; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
GO; GO:0051920; F:peroxiredoxin activity; IDA:TAIR.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Antioxidant; Chloroplast; Complete proteome; Disulfide bond;
Oxidoreductase; Peroxidase; Plastid; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 65 Chloroplast. {ECO:0000250}.
CHAIN 66 266 2-Cys peroxiredoxin BAS1, chloroplastic.
/FTId=PRO_0000023784.
DOMAIN 73 232 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 119 119 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:Q06830}.
DISULFID 119 119 Interchain (with C-241); in linked form.
{ECO:0000250|UniProtKB:Q06830}.
DISULFID 241 241 Interchain (with C-119); in linked form.
{ECO:0000250|UniProtKB:Q06830}.
CONFLICT 83 83 E -> K (in Ref. 1; CAA63909/CAA71503).
{ECO:0000305}.
CONFLICT 101 101 I -> N (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 122 122 Missing (in Ref. 1; CAA66484).
{ECO:0000305}.
CONFLICT 174 175 DV -> YF (in Ref. 7; AAM64537).
{ECO:0000305}.
CONFLICT 192 192 I -> IGI (in Ref. 2). {ECO:0000305}.
CONFLICT 218 218 R -> Q (in Ref. 7; AAM64537).
{ECO:0000305}.
CONFLICT 233 235 IQE -> TG (in Ref. 1; CAA63909/CAA71503).
{ECO:0000305}.
CONFLICT 247 247 P -> S (in Ref. 1; CAA63909/CAA71503).
{ECO:0000305}.
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


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