NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/3.3.109; PubMed=8905231 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions.";
DNA Res. 3:109-136(1996).

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
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

BA000022; BAA18344.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S75885; S75885.

RefSeq

NP_441664.1; -.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

P74250.

Protein family/group databases

PeroxiBase

3755; SYspGPx01.

Enzyme and pathway databases

BioCyc

SSP1148:SLR1171-MON; -.

Ontologies

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; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P74250.

Genome annotation databases

GeneID

954977; -.

GenomeReviews

BA000022_GR; slr1171.

KEGG

syn:slr1171; -.

NMPDR

fig|1148.1.peg.1765; -.

Phylogenomic databases

HOGENOM

P74250; -.

Genome annotation databases

CMR

P74250; slr1171.

Other

UniRef

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

Keywords

Complete proteome; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 169`	`169`	`Putative glutathione peroxidase.`	`PRO_0000066663`
`ACT_SITE`	`41 41`		`By similarity.`

Sequence information

Length: 169 AA [This is the length of the unprocessed precursor]

Molecular weight: 18452 Da [This is the MW of the unprocessed precursor]

CRC64: 0DC382089FCE39E2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAQANNTIY GFSANALDGS PVALRDFEGK VLLIVNTASQ CGFTPQYQGL QALYNRFGDR 

        70         80         90        100        110        120 
GFTVLGFPCN QFGQQEPGGS GEIKNFCETR YGVTFPLFEK VEVNGPNAHP LFKFLTAASP 

       130        140        150        160 
GMAIPFLGGA EDIKWNFTKF LVDRQGKVVK RYGSIAKPDE IAADIEKLL

P74250 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