Reviewed,
UniProtKB/Swiss-Prot P43783 (GSHR_HAEIN)
Last modified
June 16, 2009.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Glutathione reductase Short name=GRase Short name=GR EC=1.8.1.7 | ||||
| Gene names |
| ||||
| Organism | Haemophilus influenzae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 727 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 456 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 By similarity. |
| 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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH 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 – 456 | 456 | Glutathione reductase | PRO_0000067976 | |||||||
Regions | |||||||||||
| Nucleotide binding | 34 – 42 | 9 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 445 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 42 ↔ 47 | Redox-active By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | Barcak G.J., Heimer S.R. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
| [2] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
Cross-references
Sequence databases | |
|---|---|
| U20229 Genomic DNA. Translation: AAA62137.1. L42023 Genomic DNA. Translation: AAC21833.1. | |
| PIR | A64052. |
| RefSeq | NP_438331.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ALG based on UniProtKB P00390. |
| SMR | P43783. Positions 2-456. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 951071. |
| GenomeReviews | Gene locus HI0161 in contig L42023_GR. |
| KEGG | hin:HI0161. |
| NMPDR | fig|71421.1.peg.152. |
| TIGR | HI0161. |
Phylogenomic databases | |
| HOGENOM | P43783. |
| OMA | P43783. HRQPCKM. |
Enzyme and pathway databases | |
| BioCyc | HINF71421:HI_0161-MON. |
| BRENDA | 1.8.1.7. 109. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glut_reduct_1. IPR000815. Hg_reductase. 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. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01421. gluta_reduc_1. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSHR_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P43783 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


