O04955 (GSHRC_BRARP) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 85.
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, cytosolic Short name=GR Short name=GRase EC=1.8.1.7 | ||
| Gene names |
| ||
| Organism | Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis) | ||
| Taxonomic identifier | 51351 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Brassiceae › Brassica › ![]() |
Protein attributes
| Sequence length | 502 AA. |
| Sequence status | Complete. |
| 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 Potential. |
| Induction | By paraquat and ozone. Ref.1 |
| 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 |
| 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 – 502 | 502 | Glutathione reductase, cytosolic | PRO_0000067962 | |||||||
Regions | |||||||||||
| Nucleotide binding | 67 – 76 | 10 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 475 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 237 | 1 | NADP By similarity | ||||||||
| Binding site | 243 | 1 | NADP By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 76 ↔ 81 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Molecular cloning and characterization of the gene encoding glutathione reductase in Brassica campestris." Lee H.S., Jo J.K., Son D.Y. Biochim. Biophys. Acta 1395:309-314(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: cv. Seoul. Tissue: Leaf. |
| [2] | Lee H.S., Chung M.S., Jo J.K., Son D.Y. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "Genomic cloning and its expression analysis of glutathione reductase from Brassica campestris var. Pekinensis." Lee H.S., Lee B., Won S., Jo J.K. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Seoul. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF008441 mRNA. Translation: AAC49980.2. AF255651 Genomic DNA. Translation: AAF67753.1. |
| PIR | T14394. |
3D structure databases | |
| ProteinModelPortal | O04955. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.30.390.30. 1 hit. |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006324. Glut-diS_reduct. 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 | TIGR01424. gluta_reduc_2. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSHRC_BRARP | ||||||||
| Accession | Primary (citable) accession number: O04955 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
