P48638 (GSHR_NOSS1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 101.
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 | Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 103690 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc![]() |
Protein attributes
| Sequence length | 459 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Maintains high levels of reduced glutathione in the cytosol. |
| Catalytic activity | 2 glutathione + NADP+ = glutathione disulfide + NADPH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | |
| 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 |
| 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 – 459 | 459 | Glutathione reductase | PRO_0000067973 | |||||||
Regions | |||||||||||
| Nucleotide binding | 34 – 42 | 9 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 448 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 42 ↔ 47 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 234 | 1 | E → Q in CAA61856. Ref.1 | ||||||||
| Sequence conflict | 340 | 1 | R → L in CAA61856. Ref.1 | ||||||||
| Sequence conflict | 361 | 1 | V → L in CAA61856. Ref.1 | ||||||||
| Sequence conflict | 372 | 1 | L → H in CAA61856. Ref.1 | ||||||||
| Sequence conflict | 381 – 383 | 3 | RTR → AP in CAA61856. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120." Jiang F., Hellman U., Sroga G.E., Bergman B., Mannervik B. J. Biol. Chem. 270:22882-22889(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. Tabata S.DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7120 / UTEX 2576. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X89712 Genomic DNA. Translation: CAA61856.1. BA000019 Genomic DNA. Translation: BAB76667.1. |
| PIR | AH2426. I39477. |
| RefSeq | NP_489008.1. NC_003272.1. |
3D structure databases | |
| ProteinModelPortal | P48638. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 103690.all4968. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB76667; BAB76667; BAB76667. |
| GeneID | 1108569. |
| KEGG | ana:all4968. |
| PATRIC | 22780609. VBINosSp37423_5746. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1249. |
| HOGENOM | HOG000276712. |
| KO | K00383. |
| OMA | DEKTLMK. |
| ProtClustDB | PRK06116. |
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 | GSHR_NOSS1 | ||||||||
| Accession | Primary (citable) accession number: P48638 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
