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P11804 (GSHR_SPISP) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione reductase

Short name=GR
Short name=GRase
EC=1.8.1.7
OrganismSpirulina sp.
Taxonomic identifier1157 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesSpirulina

Protein attributes

Sequence length58 AA.
Sequence statusFragments.
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
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione-disulfide reductase activity

Inferred from electronic annotation. Source: UniProtKB-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 Ref.1

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
P11804 [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.

Cross-references

Sequence databases

PIRPX0017.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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: October 16, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families