O15770 (GSHR_PLAF7) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 92.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutathione reductase Short name=GR Short name=GRase EC=1.8.1.7 | ||||
| Gene names |
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| Organism | Plasmodium falciparum (isolate 3D7) [Reference proteome] | ||||
| Taxonomic identifier | 36329 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania) › ![]() |
Protein attributes
| Sequence length | 500 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 500 | 499 | Glutathione reductase | PRO_0000067960 | |||||||
Regions | |||||||||||
| Nucleotide binding | 32 – 40 | 9 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 485 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 40 ↔ 45 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 283 | 1 | E → G in AAB84117. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Glutathione reductase from Plasmodium falciparum." Gilberger T.-W., Walter R.D., Mueller S. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Genome sequence of the human malaria parasite Plasmodium falciparum." Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S. Barrell B.G.Nature 419:498-511(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Isolate 3D7. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF027825 mRNA. Translation: AAB84117.1. AE014187 Genomic DNA. Translation: AAN36804.1. |
| RefSeq | XP_001348365.1. XM_001348329.1. |
3D structure databases | |
| ProteinModelPortal | O15770. |
| SMR | O15770. Positions 2-496. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 5833.PF14_0192-1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblProtists | PF14_0192:mRNA; PF14_0192:pep; PF14_0192. |
| GeneID | 811773. |
| KEGG | pfa:PF14_0192. |
Organism-specific databases | |
| EuPathDB | PlasmoDB:PF3D7_1419800.1. |
Phylogenomic databases | |
| HOGENOM | HOG000276712. |
| KO | K00383. |
| OMA | ACAVFSI. |
Family and domain databases | |
| Gene3D | 3.30.390.30. 1 hit. |
| InterPro | IPR016156. 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] |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. |
| SUPFAM | SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | O15770. |
| ChEMBL | CHEMBL5061. |
Entry information
| Entry name | GSHR_PLAF7 | ||||||||
| Accession | Primary (citable) accession number: O15770 Secondary accession number(s): Q8ILQ2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
