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Reviewed, UniProtKB/Swiss-Prot P11804 (GSHR_SPISP)

Last modified November 4, 2008. Version 52. 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:
    Glutathione reductase
      Short name=GRase
      Short name=GR
    EC=1.8.1.7
OrganismSpirulina sp.
Taxonomic identifier1157 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatorialesSpirulina

Protein attributes

Sequence length58 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activity

2 glutathione + NADP(+) = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subcellular location

Cytoplasm.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords

   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglutathione-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›58›58Glutathione reductase
PRO_0000067978

Regions

Nucleotide binding5 – 139FAD By similarity

Amino acid modifications

Disulfide bond13 ↔ 18Redox-active

Experimental info

Non-adjacent residues21 – 222
Non-adjacent residues43 – 442
Non-terminal residue11
Non-terminal residue581

Sequences

Sequence LengthMass (Da)Tools
P11804-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: B2C2A050EF55B5EF

FASTA585,952
        10         20         30         40         50 
VAIAENSVVG GTCVIRGCVP KLTLTGDDTE PLIVDALLCA TGRTTQSNIF AVGDCTDR 

« Hide

References

[1]"Isolation and sequence studies of cysteinyl peptides from Spirulina glutathione reductase: comparison of active site cysteine peptides with those of other flavoprotein disulfide oxidoreductases."
Cui J.-Y., Wakabayashi S., Wada K., Fukuyama K., Matsubara H.
J. Biochem. 105:390-394(1989) [PubMed: 2499573] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.

Cross-references

Sequence databases

PIRPX0017.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHR_SPISP
AccessionPrimary (citable) accession number: P11804
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 4, 2008
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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