Reviewed, UniProtKB/Swiss-Prot Q96468 (BAS1_HORVU)

Names and origin

Protein names

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

Gene names

Name:

BAS1

Organism

Hordeum vulgare (Barley)

Taxonomic identifier

4513 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	210 AA.
Sequence status	Fragment.
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 important in the developing shoot and photosynthesizing leaf.
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.
Tissue specificity	Expressed in leaf blade, sheath, basiplast, stem and green spike. Maximal expression in young developing shoots segments where cell division and elongation take place. Not expressed in roots.
Developmental stage	Maximal levels are seen in 4-day old seedlings and decline during aging of the seedling.
Post-translational modification	The Cys-64-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-64 (probably Cys-SOH) rapidly reacts with Cys-185-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
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 10	›10	Chloroplast By similarity
	Chain	11 – 210	200	2-Cys peroxiredoxin BAS1, chloroplastic		PRO_0000023785
Regions
	Domain	18 – 177	160	Thioredoxin
Sites
	Active site	64	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Disulfide bond	64		Interchain (with C-185); in linked form By similarity
	Disulfide bond	185		Interchain (with C-64); in linked form By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q96468-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 4DD488179D6BCAC9	FASTA	210	23,299
	10 20 30 40 50 60 DARARSFVAR AAAEYDLPLV GNKAPDFAAE AVFDQEFINV KLSDYIGKKY VILFFYPLDF 70 80 90 100 110 120 TFVCPTEITA FSDRHEEFEK INTEILGVSV DSVFSHLAWV QTERKSGGLG DLKYPLVSDV 130 140 150 160 170 180 TKSISKSFGV LIPDQGIALR GLFIIDKEGV IQHSTINNLG IGRSVDETLR TLQALQYVKK 190 200 210 PDEVCPAGWK PGEKSMKPDP KGSKEYFAAI

References

[1]

"Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases." Baier M., Dietz K.-J. Plant Mol. Biol. 31:553-564(1996) [PubMed: 8790288] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Gerbel. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z34917 mRNA. Translation: CAA84396.1.
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
SMR	Q96468. Positions 20-208.
ModBase	Search...
Organism-specific databases
Gramene	Q96468.
Enzyme and pathway databases
BRENDA	1.11.1.15. 283.
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

BAS1_HORVU

Accession

Primary (citable) accession number: Q96468

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)