Q873E8 (GSHR_NEUCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 72.
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 | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome] | ||||
| Taxonomic identifier | 367110 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › ![]() |
Protein attributes
| Sequence length | 468 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. |
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 response to oxidative stressInferred from electronic annotation. Source: EnsemblFungi glutathione metabolic processInferred from electronic annotation. Source: InterPro protein glutathionylationInferred from electronic annotation. Source: EnsemblFungi |
| Cellular_component | mitochondrion Inferred from electronic annotation. Source: EnsemblFungi nucleusInferred from electronic annotation. Source: EnsemblFungi |
| 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 – 468 | 468 | Glutathione reductase | PRO_0000067969 | |||||||
Regions | |||||||||||
| Nucleotide binding | 38 – 46 | 9 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 457 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 46 ↔ 51 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987. |
| [2] | "The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. Birren B.W.Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX284749 Genomic DNA. Translation: CAD70360.1. AABX02000008 Genomic DNA. Translation: EAA27212.1. |
| RefSeq | XP_956448.1. XM_951355.1. |
| UniGene | Ncr.16209. |
3D structure databases | |
| ProteinModelPortal | Q873E8. |
| SMR | Q873E8. Positions 6-468. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 5141.NCU03339.1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | EFNCRT00000002546; EFNCRP00000002546; EFNCRG00000002543. |
| GeneID | 3872613. |
| KEGG | ncr:NCU03339. |
Phylogenomic databases | |
| eggNOG | COG1249. |
| HOGENOM | HOG000276712. |
| KO | K00383. |
| OMA | VTSHRQP. |
| 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_NEUCR | ||||||||
| Accession | Primary (citable) accession number: Q873E8 Secondary accession number(s): Q1K529 | ||||||||
| 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
