Q6BPI1 (GSHR_DEBHA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 70.
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 | Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome] | ||||
| Taxonomic identifier | 284592 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces › ![]() |
Protein attributes
| Sequence length | 490 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 By similarity. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
| Sequence caution | The sequence CAG88130.2 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide bindingInferred 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 490 | 490 | Glutathione reductase | PRO_0000067967 | |||||||
Regions | |||||||||||
| Nucleotide binding | 39 – 49 | 11 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 479 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 49 ↔ 54 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR382137 Genomic DNA. Translation: CAG88130.2. Different initiation. |
| RefSeq | XP_459889.2. XM_459889.2. |
3D structure databases | |
| ProteinModelPortal | Q6BPI1. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 4959.Q6BPI1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2902393. |
| KEGG | dha:DEHA2E13442g. |
Phylogenomic databases | |
| eggNOG | COG1249. |
| HOGENOM | HOG000276712. |
| KO | K00383. |
| OrthoDB | EOG415KNX. |
Family and domain databases | |
| Gene3D | 3.30.390.30. 1 hit. |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glutathione_Rdtase_euk/bac. 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. |
| TIGRFAMs | TIGR01421. gluta_reduc_1. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSHR_DEBHA | ||||||||
| Accession | Primary (citable) accession number: Q6BPI1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
