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O15770 (GSHR_PLAF7) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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
Gene names
Name:GR3
ORF Names:PF14_0192
OrganismPlasmodium falciparum (isolate 3D7) [Reference proteome]
Taxonomic identifier36329 [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 transcript 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.

Subcellular location

Cytoplasm By similarity.

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 termComplete proteome
Reference proteome
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 By similarity
Chain2 – 500499Glutathione reductase
PRO_0000067960

Regions

Nucleotide binding32 – 409FAD By similarity

Sites

Active site4851Proton acceptor By similarity

Amino acid modifications

Disulfide bond40 ↔ 45Redox-active By similarity

Experimental info

Sequence conflict2831E → G in AAB84117. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O15770 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: EFFBA1668599EA37

FASTA50056,492
        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 NLEKLNVETN NNYIVVDENQ 

       310        320        330        340        350        360 
RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEETYLNKK 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027825 mRNA. Translation: AAB84117.1.
AE014187 Genomic DNA. Translation: AAN36804.1.
RefSeqXP_001348365.1. XM_001348329.1.

3D structure databases

ProteinModelPortalO15770.
SMRO15770. Positions 2-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5833.PF14_0192-1.

Chemistry

BindingDBO15770.
ChEMBLCHEMBL5061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPF14_0192:mRNA; PF14_0192:pep; PF14_0192.
GeneID811773.
KEGGpfa:PF14_0192.

Organism-specific databases

EuPathDBPlasmoDB:PF3D7_1419800.2.

Phylogenomic databases

HOGENOMHOG000276712.
KOK00383.
OMAMFNALGT.
PhylomeDBO15770.

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...

Entry information

Entry nameGSHR_PLAF7
AccessionPrimary (citable) accession number: O15770
Secondary accession number(s): Q8ILQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 95 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families