Reviewed, UniProtKB/Swiss-Prot Q9C5R8 (BAS1B_ARATH)

Names and origin

Protein names

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

Gene names

Ordered Locus Names:	At5g06290
ORF Names:	MHF15.19

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation By similarity.
Subcellular location	Plastid › chloroplast By similarity.
Induction	Down-regulated by ascorbate. Ref.3
Post-translational modification	The Cys-124-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-124 (probably Cys-SOH) rapidly reacts with Cys-246-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 stroma Inferred from direct assay. Source: TAIR
Molecular function	peroxiredoxin activity Ref.3 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 – 70	70	Chloroplast By similarity
	Chain	71 – 271	201	2-Cys peroxiredoxin BAS1-like, chloroplastic		PRO_0000284083
Regions
	Domain	78 – 237	160	Thioredoxin
Sites
	Active site	124	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Disulfide bond	124		Interchain (with C-246); in linked form By similarity
	Disulfide bond	246		Interchain (with C-124); in linked form By similarity
Experimental info
	Sequence conflict	215	1	T → P in AAG40040. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9C5R8-1 [UniParc]. Last modified April 17, 2007. Version 2. Checksum: A15B6EFC893B460B	FASTA	271	29,562
	10 20 30 40 50 60 MASIASSSST TLLSSSRVLL PSKSSLLSPT VSFPRIIPSS SASSSSLCSG FSSLGSLTTN 70 80 90 100 110 120 RSASRRNFAV KAQADDLPLV GNKAPDFEAE AVFDQEFIKV KLSEYIGKKY VILFFYPLDF 130 140 150 160 170 180 TFVCPTEITA FSDRYEEFEK LNTEVLGVSV DSVFSHLAWV QTDRKSGGLG DLNYPLVSDI 190 200 210 220 230 240 TKSISKSFGV LIPDQGIALR GLFIIDKEGV IQHSTINNLG IGRSVDETMR TLQALQYVQE 250 260 270 NPDEVCPAGW KPGEKSMKPD PKLSKEYFSA I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones." Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:291-300(1997) [PubMed: 9405937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"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.
[4]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB006700 Genomic DNA. Translation: BAB08951.1. AF324689 mRNA. Translation: AAG40040.2. AF326871 mRNA. Translation: AAG41453.1. Different initiation. AF339693 mRNA. Translation: AAK00375.1. Different initiation. AY054621 mRNA. Translation: AAK96812.1. Different initiation. AY081503 mRNA. Translation: AAM10065.1. Different initiation.
IPI	IPI00539263.
UniGene	At.7277
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
ModBase	Search...
Protein family/group databases
PeroxiBase	4361. At2CysPrxB.
Proteomic databases
PRIDE	Q9C5R8.
Genome annotation databases
GenomeReviews	Gene locus AT5G06290 in contig BA000015_GR.
NMPDR	fig|3702.1.peg.22752.
Organism-specific databases
TAIR	At5g06290.
Enzyme and pathway databases
BRENDA	1.11.1.15. 302.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. 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

BAS1B_ARATH

Accession

Primary (citable) accession number: Q9C5R8
Secondary accession number(s): Q9FED5, Q9FNH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	April 17, 2007
Last modified:	June 16, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)