[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=LMG P-15151; Hazbon M.H., Dufel H., Cornelis P., Jaeger K.E.; "Molecular characterization of an operon from Pseudomonas wisconsinensis responsible for the production of an extracellular lipase."; Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBCELLULAR LOCATION: Periplasm.
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

U88907; AAB53646.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O08368.

Protein family/group databases

PeroxiBase

3743; PwGPx01.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
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; FALSE_NEG.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

O08368.

UniRef

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

Keywords

Oxidoreductase; Periplasm; Peroxidase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`CHAIN`	`23 222`	`200`	`Glutathione peroxidase.`	`PRO_0000013095`
`ACT_SITE`	`61 61`		`By similarity.`

Sequence information

Length: 222 AA [This is the length of the unprocessed precursor]

Molecular weight: 24742 Da [This is the MW of the unprocessed precursor]

CRC64: 04A89ABC21E777CB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIRRLACSL LLSSLALPVL AAECPAMLQG ELPKLRAKGE NIELCQYAGK PLVVVNTASF 

        70         80         90        100        110        120 
CGFTPQFKGL EALYQRYKDQ ELEVLGVPSD DFRQESADSK ETATVCYVNY GVTFAMTEPQ 

       130        140        150        160        170        180 
PVSGANAIPL FKGLAEQSRQ PRWNFFKYVV DRQGKVVASF SSLTKPDDPE LIAARREGDR 

       190        200        210        220 
LATLIPSRFT ALHPSGRWAL SVCLPRLARR RTQFTRRALQ EQ

O08368 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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