Reviewed, UniProtKB/Swiss-Prot Q96291 (BAS1A_ARATH)

Names and origin

Protein names

Recommended name:
    2-Cys peroxiredoxin BAS1, chloroplastic
      Short name=2-Cys peroxiredoxin A
      Short name=2-Cys Prx A
    EC=1.11.1.15
Alternative name(s):
    Thiol-specific antioxidant protein A

Gene names

Name:	BAS1
Ordered Locus Names:	At3g11630
ORF Names:	T19F11.3, F24K9.28

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf. Involved in the detoxification of alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Ref.7
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation By similarity. Interacts with the plastidial thioredoxin CDSP32. Interacts with the plastidial NADPH-dependent thioredoxin reductase ANTR-C. Ref.7 Ref.10
Subcellular location	Plastid › chloroplast Ref.2.
Induction	Down-regulated under highly reduced cellular thiol pool conditions. Down-regulated by ascorbate. Slightly induced by oxidative stress. Ref.8
Post-translational modification	The Cys-119-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-119 (probably Cys-SOH) rapidly reacts with Cys-241-SH of the other subunit to form an intermolecular disulfide. This disulfide might subsequently be reduced by thioredoxin By similarity.
Sequence similarities	Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Redox-active center Transit peptide
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro defense response to bacterium Inferred from expression pattern. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cold Inferred from expression pattern. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR stromule Inferred from direct assay. Source: TAIR thylakoid Inferred from direct assay. Source: TAIR
Molecular function	peroxiredoxin activity Ref.8 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 65	65	Chloroplast By similarity
	Chain	66 – 266	201	2-Cys peroxiredoxin BAS1, chloroplastic		PRO_0000023784
Regions
	Domain	73 – 232	160	Thioredoxin
Sites
	Active site	119	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Disulfide bond	119		Interchain (with C-241); in linked form By similarity
	Disulfide bond	241		Interchain (with C-119); in linked form By similarity
Experimental info
	Sequence conflict	83	1	E → K in CAA63909. Ref.1
	Sequence conflict	83	1	E → K in CAA71503. Ref.1
	Sequence conflict	101	1	I → N Ref.1
	Sequence conflict	101	1	I → N Ref.2
	Sequence conflict	122	1	Missing in CAA66484. Ref.1
	Sequence conflict	174 – 175	2	DV → YF in AAM64537. Ref.6
	Sequence conflict	192	1	I → IGI Ref.2
	Sequence conflict	218	1	R → Q in AAM64537. Ref.6
	Sequence conflict	233 – 235	3	IQE → TG in CAA63909. Ref.1
	Sequence conflict	233 – 235	3	IQE → TG in CAA71503. Ref.1
	Sequence conflict	247	1	P → S in CAA63909. Ref.1
	Sequence conflict	247	1	P → S in CAA71503. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q96291-1 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 2CEB476A1A8694AD	FASTA	266	29,092
	10 20 30 40 50 60 MASVASSTTL ISSPSSRVFP AKSSLSSPSV SFLRTLSSPS ASASLRSGFA RRSSLSSTSR 70 80 90 100 110 120 RSFAVKAQAD DLPLVGNKAP DFEAEAVFDQ EFIKVKLSDY IGKKYVILFF YPLDFTFVCP 130 140 150 160 170 180 TEITAFSDRH SEFEKLNTEV LGVSVDSVFS HLAWVQTDRK SGGLGDLNYP LISDVTKSIS 190 200 210 220 230 240 KSFGVLIHDQ GIALRGLFII DKEGVIQHST INNLGIGRSV DETMRTLQAL QYIQENPDEV 250 260 CPAGWKPGEK SMKPDPKLSK EYFSAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"2-Cys peroxiredoxin bas1 from Arabidopsis thaliana." Baier M., Dietz K.-J. Plant Gene Register PGR96-031 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"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." Baier M., Dietz K.-J. Plant J. 12:179-190(1997) [PubMed: 9263459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION. Strain: cv. Columbia.
[3]	Baier M. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." 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. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage." Broin M., Cuine S., Eymery F., Rey P. Plant Cell 14:1417-1432(2002) [PubMed: 12084836] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDSP32.
[8]	"Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis." Horling F., Lamkemeyer P., Koenig J., Finkemeier I., Kandlbinder A., Baier M., Dietz K.-J. Plant Physiol. 131:317-325(2003) [PubMed: 12529539] [Abstract] Cited for: INDUCTION.
[9]	"The plant multigenic family of thiol peroxidases." Rouhier N., Jacquot J.-P. Free Radic. Biol. Med. 38:1413-1421(2005) [PubMed: 15890615] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
[10]	"The C-type Arabidopsis thioredoxin reductase ANTR-C acts as an electron donor to 2-Cys peroxiredoxins in chloroplasts." 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. Biochem. Biophys. Res. Commun. 348:478-484(2006) [PubMed: 16884685] [Abstract] Cited for: INTERACTION WITH ANTR-C.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X94218 mRNA. Translation: CAA63909.1. Y10478 mRNA. Translation: CAA71503.1. X97910 Genomic DNA. Translation: CAA66484.2. AC009918 Genomic DNA. Translation: AAF02131.1. AC008153 Genomic DNA. Translation: AAG51430.1. AF324996 mRNA. Translation: AAG40348.1. AF419578 mRNA. Translation: AAL31910.1. AY079107 mRNA. Translation: AAL84991.1. AY086974 mRNA. Translation: AAM64537.1.
IPI	IPI00526535.
RefSeq	NP_187769.1.
UniGene	At.22950 At.68687 Rra.17341 Rra.5878 Rsa.7248
3D structure databases
SMR	Q96291. Positions 75-264.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96291.
Protein family/group databases
PeroxiBase	4358. At2CysPrxA.
Proteomic databases
PRIDE	Q96291.
ProMEX	Q96291.
Genome annotation databases
GeneID	820335.
GenomeReviews	Gene locus AT3G11630 in contig BA000014_GR.
KEGG	ath:AT3G11630.
NMPDR	fig|3702.1.peg.13221.
Organism-specific databases
TAIR	At3g11630.
Phylogenomic databases
eggNOG	KOG0852.
HOGENOM	HBG493509.
InParanoid	Q96291.
OMA	KAWINTS.
PhylomeDB	Q96291.
Enzyme and pathway databases
BRENDA	1.11.1.15. 302.
Gene expression databases
ArrayExpress	Q96291.
Genevestigator	Q96291.
GermOnline	AT3G11630. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BAS1A_ARATH

Accession

Primary (citable) accession number: Q96291
Secondary accession number(s): P92938, Q8L5U1, Q9S7Y0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 11, 2001
Last modified:	February 9, 2010
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)