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Q94655 (GSHR_PLAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:GR2
OrganismPlasmodium falciparum (isolate K1 / Thailand)
Taxonomic identifier5839 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Maintains high levels of reduced glutathione in the cytosol By similarity.

Catalytic activity

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer.

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 term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

glutathione-disulfide reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 500499Glutathione reductase
PRO_0000067959

Regions

Nucleotide binding32 – 409FAD By similarity

Sites

Active site4851Proton acceptor By similarity

Amino acid modifications

Disulfide bond40 ↔ 45Redox-active By similarity

Secondary structure

.............................................................................. 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q94655 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AB2299144002FCD3

FASTA50056,561
        10         20         30         40         50         60 
MVYDLIVIGG GSGGMAAARR AARHNAKVAL VEKSRLGGTC VNVGCVPKKI MFNAASVHDI 

        70         80         90        100        110        120 
LENSRHYGFD TKFSFNLPLL VERRDKYIQR LNNIYRQNLS KDKVDLYEGT ASFLSENRIL 

       130        140        150        160        170        180 
IKGTKDNNNK DNGPLNEEIL EGRNILIAVG NKPVFPPVKG IENTISSDEF FNIKESKKIG 

       190        200        210        220        230        240 
IVGSGYIAVE LINVIKRLGI DSYIFARGNR ILRKFDESVI NVLENDMKKN NINIVTFADV 

       250        260        270        280        290        300 
VEIKKVSDKN LSIHLSDGRI YEHFDHVIYC VGRSPDTENL KLEKLNVETN NNYIVVDENQ 

       310        320        330        340        350        360 
RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEERYLNKK ENVTEDIFYN VQLTPVAINA 

       370        380        390        400        410        420 
GRLLADRLFL KKTRKTNYKL IPTVIFSHPP IGTIGLSEEA AIQIYGKENV KIYESKFTNL 

       430        440        450        460        470        480 
FFSVYDIEPE LKEKTYLKLV CVGKDELIKG LHIIGLNADE IVQGFAVALK MNATKKDFDE 

       490        500 
TIPIHPTAAE EFLTLQPWMK 

« Hide

References

[1]"Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum."
Faerber P.M., Becker K., Mueller S.
Eur. J. Biochem. 239:655-661(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria."
Krauth-Siegel R.L., Muller J.G., Lottspeich F., Schirmer R.H.
Eur. J. Biochem. 235:345-350(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X93462 Genomic DNA. Translation: CAA63747.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONFX-ray2.60A1-500[»]
ProteinModelPortalQ94655.
SMRQ94655. Positions 2-496.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1741261.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1249.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ94655.

Entry information

Entry nameGSHR_PLAFK
AccessionPrimary (citable) accession number: Q94655
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references