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P11804

- GSHR_SPISP

UniProt

P11804 - GSHR_SPISP

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Protein

Glutathione reductase

Gene
N/A
Organism
Spirulina sp.
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi5 – 139FADBy similarity

GO - Molecular functioni

  1. glutathione-disulfide reductase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
OrganismiSpirulina sp.
Taxonomic identifieri1157 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesSpirulina

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›58›58Glutathione reductasePRO_0000067978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi13 ↔ 18Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

InterProiIPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

P11804-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
VAIAENSVVG GTCVIRGCVP KLTLTGDDTE PLIVDALLCA TGRTTQSNIF

AVGDCTDR
Length:58
Mass (Da):5,952
Last modified:October 1, 1989 - v1
Checksum:iB2C2A050EF55B5EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi21 – 222Curated
Non-adjacent residuesi43 – 442Curated
Non-terminal residuei58 – 581

Sequence databases

PIRiPX0017.

Cross-referencesi

Sequence databases

PIRi PX0017.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view ]
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGSHR_SPISP
AccessioniPrimary (citable) accession number: P11804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 26, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3