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Protein

2-Cys peroxiredoxin BAS1, chloroplastic

Gene

BAS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei119 – 1191Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  • peroxidase activity Source: UniProtKB
  • peroxiredoxin activity Source: TAIR

GO - Biological processi

  • defense response to bacterium Source: TAIR
  • response to cold Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciARA:AT3G11630-MONOMER.
BRENDAi1.11.1.15. 399.
ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.
R-ATH-5628897. TP53 Regulates Metabolic Genes.

Protein family/group databases

PeroxiBasei4358. At2CysPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
2-Cys peroxiredoxin BAS1, chloroplastic (EC:1.11.1.15)
Short name:
2-Cys Prx A
Short name:
2-Cys peroxiredoxin A
Alternative name(s):
Thiol-specific antioxidant protein A
Gene namesi
Name:BAS1
Ordered Locus Names:At3g11630
ORF Names:F24K9.28, T19F11.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G11630.

Subcellular locationi

  • Plastidchloroplast 1 Publication

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • stromule Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565ChloroplastBy similarityAdd
BLAST
Chaini66 – 2662012-Cys peroxiredoxin BAS1, chloroplasticPRO_0000023784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi119 – 119Interchain (with C-241); in linked formBy similarity
Disulfide bondi241 – 241Interchain (with C-119); in linked formBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ96291.
PRIDEiQ96291.

PTM databases

iPTMnetiQ96291.

Expressioni

Inductioni

Down-regulated under highly reduced cellular thiol pool conditions. Down-regulated by ascorbate. Slightly induced by oxidative stress.1 Publication

Gene expression databases

GenevisibleiQ96291. AT.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation (By similarity). Interacts with the plastidial thioredoxin CDSP32. Interacts with the plastidial NADPH-dependent thioredoxin reductase ANTR-C.By similarity2 Publications

Protein-protein interaction databases

BioGridi5669. 10 interactions.
IntActiQ96291. 7 interactions.
STRINGi3702.AT3G11630.1.

Structurei

3D structure databases

ProteinModelPortaliQ96291.
SMRiQ96291. Positions 75-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 232160ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
HOGENOMiHOG000022343.
InParanoidiQ96291.
KOiK03386.
OMAiVQPFKTE.
PhylomeDBiQ96291.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96291-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVASSTTL ISSPSSRVFP AKSSLSSPSV SFLRTLSSPS ASASLRSGFA
60 70 80 90 100
RRSSLSSTSR RSFAVKAQAD DLPLVGNKAP DFEAEAVFDQ EFIKVKLSDY
110 120 130 140 150
IGKKYVILFF YPLDFTFVCP TEITAFSDRH SEFEKLNTEV LGVSVDSVFS
160 170 180 190 200
HLAWVQTDRK SGGLGDLNYP LISDVTKSIS KSFGVLIHDQ GIALRGLFII
210 220 230 240 250
DKEGVIQHST INNLGIGRSV DETMRTLQAL QYIQENPDEV CPAGWKPGEK
260
SMKPDPKLSK EYFSAI
Length:266
Mass (Da):29,092
Last modified:July 11, 2001 - v2
Checksum:i2CEB476A1A8694AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831E → K in CAA63909 (Ref. 1) Curated
Sequence conflicti83 – 831E → K in CAA71503 (Ref. 1) Curated
Sequence conflicti101 – 1011I → N (Ref. 1) Curated
Sequence conflicti101 – 1011I → N (PubMed:9263459).Curated
Sequence conflicti122 – 1221Missing in CAA66484 (Ref. 1) Curated
Sequence conflicti174 – 1752DV → YF in AAM64537 (Ref. 7) Curated
Sequence conflicti192 – 1921I → IGI (PubMed:9263459).Curated
Sequence conflicti218 – 2181R → Q in AAM64537 (Ref. 7) Curated
Sequence conflicti233 – 2353IQE → TG in CAA63909 (Ref. 1) Curated
Sequence conflicti233 – 2353IQE → TG in CAA71503 (Ref. 1) Curated
Sequence conflicti247 – 2471P → S in CAA63909 (Ref. 1) Curated
Sequence conflicti247 – 2471P → S in CAA71503 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94218 mRNA. Translation: CAA63909.1.
Y10478 mRNA. Translation: CAA71503.1.
X97910 Genomic DNA. Translation: CAA66484.2.
AC008153 Genomic DNA. Translation: AAG51430.1.
AC009918 Genomic DNA. Translation: AAF02131.1.
CP002686 Genomic DNA. Translation: AEE75077.1.
AF324996 mRNA. Translation: AAG40348.1.
AF419578 mRNA. Translation: AAL31910.1.
AY079107 mRNA. Translation: AAL84991.1.
AY086974 mRNA. Translation: AAM64537.1.
RefSeqiNP_187769.1. NM_111995.2.
UniGeneiAt.22950.
At.68687.

Genome annotation databases

EnsemblPlantsiAT3G11630.1; AT3G11630.1; AT3G11630.
GeneIDi820335.
GrameneiAT3G11630.1; AT3G11630.1; AT3G11630.
KEGGiath:AT3G11630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94218 mRNA. Translation: CAA63909.1.
Y10478 mRNA. Translation: CAA71503.1.
X97910 Genomic DNA. Translation: CAA66484.2.
AC008153 Genomic DNA. Translation: AAG51430.1.
AC009918 Genomic DNA. Translation: AAF02131.1.
CP002686 Genomic DNA. Translation: AEE75077.1.
AF324996 mRNA. Translation: AAG40348.1.
AF419578 mRNA. Translation: AAL31910.1.
AY079107 mRNA. Translation: AAL84991.1.
AY086974 mRNA. Translation: AAM64537.1.
RefSeqiNP_187769.1. NM_111995.2.
UniGeneiAt.22950.
At.68687.

3D structure databases

ProteinModelPortaliQ96291.
SMRiQ96291. Positions 75-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5669. 10 interactions.
IntActiQ96291. 7 interactions.
STRINGi3702.AT3G11630.1.

Protein family/group databases

PeroxiBasei4358. At2CysPrx01.

PTM databases

iPTMnetiQ96291.

Proteomic databases

PaxDbiQ96291.
PRIDEiQ96291.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G11630.1; AT3G11630.1; AT3G11630.
GeneIDi820335.
GrameneiAT3G11630.1; AT3G11630.1; AT3G11630.
KEGGiath:AT3G11630.

Organism-specific databases

TAIRiAT3G11630.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
HOGENOMiHOG000022343.
InParanoidiQ96291.
KOiK03386.
OMAiVQPFKTE.
PhylomeDBiQ96291.

Enzyme and pathway databases

BioCyciARA:AT3G11630-MONOMER.
BRENDAi1.11.1.15. 399.
ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.
R-ATH-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

PROiQ96291.

Gene expression databases

GenevisibleiQ96291. AT.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "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].
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDSP32.
  9. "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] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "The plant multigenic family of thiol peroxidases."
    Rouhier N., Jacquot J.-P.
    Free Radic. Biol. Med. 38:1413-1421(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
  11. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANTR-C.

Entry informationi

Entry nameiBAS1A_ARATH
AccessioniPrimary (citable) accession number: Q96291
Secondary accession number(s): P92938, Q8L5U1, Q9S7Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2001
Last modified: July 6, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.