Reviewed,
UniProtKB/Swiss-Prot P48638 (GSHR_ANASP)
Last modified
November 25, 2008.
Version 65.
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 |
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| Organism | Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 103690 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc |
Protein attributes
| Sequence length | 459 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 |
| 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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro NADP bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activityInferred from electronic annotation. Source: InterPro |
| 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: 7559423] [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: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| X89712 Genomic DNA. Translation: CAA61856.1. BA000019 Genomic DNA. Translation: BAB76667.1. | |
| PIR | AH2426. I39477. |
| RefSeq | NP_489008.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ONF based on UniProtKB Q94655. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1108569. |
| GenomeReviews | Gene locus all4968 in contig BA000019_GR. |
| KEGG | ana:all4968. |
| NMPDR | fig|103690.1.peg.5275. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P48638. |
Enzyme and pathway databases | |
| BioCyc | NSP103690:ALL4968-MON. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006324. Glut_reduct_pln. IPR000815. Hg_reductase. IPR001100. Pyr_nuc-diS_OxRdtase. 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. PR00411. PNDRDTASEI. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01424. gluta_reduc_2. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSHR_ANASP | ||||||||
| Accession | Primary (citable) accession number: P48638 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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