[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Birte; PubMed=9680987 [NCBI, ExPASy, EBI, Israel, Japan] Mullineaux P.M., Karpinski S., Jimenez A., Cleary S.P., Robinson C., Creissen G.P.; "Identification of cDNAS encoding plastid-targeted glutathione peroxidase."; Plant J. 13:375-379(1998).

Comments

FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H₂O.
SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
SIMILARITY: Belongs to the glutathione peroxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ000508; CAA04142.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T06462; T06462.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

O24296.

Protein family/group databases

PeroxiBase

2897; PsGPx01.

Ontologies

GO:0047066;	Molecular function: phospholipid-hydroperoxide glutathione peroxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR11592; Glut_peroxidase; 1.

Pfam

PF00255; GSHPx; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000303; Glutathion_perox; 1.

PRINTS

PR01011; GLUTPROXDASE.

PROSITE

PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Chloroplast; Oxidoreductase; Peroxidase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 64`	`64`	`Chloroplast (Potential).`
`CHAIN`	`65 236`	`172`	`Phospholipid hydroperoxide glutathione peroxidase, chloroplastic.`	`PRO_0000013087`
`ACT_SITE`	`111 111`		`By similarity.`

Sequence information

Length: 236 AA [This is the length of the unprocessed precursor]

Molecular weight: 26400 Da [This is the MW of the unprocessed precursor]

CRC64: 85300731A3455E5D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASMAFSTTF FTPLRDFNQP RTNSTPSTSL PFTKSSIASS KSPFFQLGFS QQASSNFPIV 

        70         80         90        100        110        120 
PSKTRSFSVN AKAIKDKTIY DFTVKDIDKK DVSLSKFKGK VLLIVNVASR CGLTSSNYTE 

       130        140        150        160        170        180 
LSHLYENFKN KGLEVLAFPC NQFGMQEPGS NEEIKQFACT KFKAEFPIFD KVDVNGPFTA 

       190        200        210        220        230 
PVYQFLKSSS GGFFGDIVKW NFEKFLVDKN GKVVERYPPT TSPFQIEKDI QKLLAA

O24296 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