Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q94655 (GSHR_PLAFK)

Last modified September 2, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Initiator methionine11Removed
Chain2 – 500499Glutathione reductase

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
Q94655-1 [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: 8774709] [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: 8631352] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.

Cross-references

Sequence databases

X93462 Genomic DNA. Translation: CAA63747.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ONFX-ray2.60A1-500[»]
ModBaseSearch...

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR001100. Pyr_nuc-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
PR00411. PNDRDTASEI.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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: September 2, 2008
This is version 65 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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