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Reviewed, UniProtKB/Swiss-Prot O24364 (BAS1_SPIOL)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2-Cys peroxiredoxin BAS1, chloroplastic
    EC=1.11.1.15
Alternative name(s):
    Thiol-specific antioxidant protein
Gene names
Name: BAS1
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesAmaranthaceaeSpinacia

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

May be an antioxidant enzyme particularly 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

Plastidchloroplast By similarity.

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-240-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 componentChloroplast
Plastid
   DomainRedox-active center
Transit peptide
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6565Chloroplast By similarity
Chain66 – 2652002-Cys peroxiredoxin BAS1, chloroplastic
PRO_0000023786

Regions

Domain73 – 232160Thioredoxin

Sites

Active site1191Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond119Interchain (with C-240); in linked form By similarity
Disulfide bond240Interchain (with C-119); in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
O24364-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 11F479093C2F573B

FASTA26528,896
        10         20         30         40         50         60 
MACVASSTTL 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 QYTGNPDEVC 

       250        260 
PAGWKPGEKS MKPDPKLSKE YFSAI 

« Hide

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].
Tissue: Leaf.

Cross-references

Sequence databases

X94219 mRNA. Translation: CAA63910.1.
PIRT09211.

3D structure databases

HSSPHSSP built from PDB template 1QMV based on UniProtKB P32119.
SMRO24364. Positions 75-263.
ModBaseSearch...

Protein-protein interaction databases

IntActO24364. 1 interaction.

Protein family/group databases

PeroxiBase4408. So2CysPrx.

Enzyme and pathway databases

BRENDA1.11.1.15. 286.

Family and domain databases

InterProIPR000866. Alkyl_hydroperoxide_Rdtase.
IPR019479. Peroxiredoxin_C.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBAS1_SPIOL
AccessionPrimary (citable) accession number: O24364
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents