Reviewed,
UniProtKB/Swiss-Prot O15770 (GSHR_PLAF7)
Last modified
September 22, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutathione reductase Short name=GRase Short name=GR EC=1.8.1.7 | ||
| Gene names |
| ||
| Organism | Plasmodium falciparum (isolate 3D7) | ||
| 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 |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred 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 | |||||||||
Sequences
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References
| [1] | Gilberger T.-W., Walter R.D., Mueller S. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF027825 mRNA. Translation: AAB84117.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ONF based on UniProtKB Q94655. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00945. HGRDTASE. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSHR_PLAF7 | ||||||||
| Accession | Primary (citable) accession number: O15770 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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