NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leaf;
DOI=10.1007/BF00042228; PubMed=8790288 [NCBI, ExPASy, EBI, Israel, Japan]
Baier M., Dietz K.-J.;
"Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases.";
Plant Mol. Biol. 31:553-564(1996).

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: Homodimer; disulfide-linked, upon oxidation (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
PTM: The Cys-119-SH group is the primary site of oxidation by H(2)O(2), 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).
SIMILARITY: Belongs to the ahpC/TSA family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

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Cross-references

Sequence databases

EMBL

X94219; CAA63910.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09211; T09211.

3D structure databases

HSSP

P32119; 1QMV. [HSSP ENTRY / PDB]

SMR

O24364; 75-263.

ModBase

O24364.

Protein family/group databases

PeroxiBase

4408; So2CysPrx.

Ontologies

GO:0051920;	Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PROSITE

PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antioxidant; Chloroplast; Oxidoreductase; Peroxidase; Plastid; Redox-active center; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 65`	`65`	`Chloroplast (By similarity).`
`CHAIN`	`66 265`	`200`	`2-Cys peroxiredoxin BAS1, chloroplastic.`	`PRO_0000023786`
`DOMAIN`	`73 232`	`160`	`Thioredoxin.`
`ACT_SITE`	`119 119`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`119 119`		`Interchain (with C-240); in linked form (By similarity).`
`DISULFID`	`240 240`		`Interchain (with C-119); in linked form (By similarity).`

Sequence information

Length: 265 AA [This is the length of the unprocessed precursor]

Molecular weight: 28896 Da [This is the MW of the unprocessed precursor]

CRC64: 11F479093C2F573B [This is a checksum on the sequence]

        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

O24364 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools