Reviewed,
UniProtKB/Swiss-Prot Q47951 (DHE3_PYREN)
Last modified
November 25, 2008.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Glutamate dehydrogenase Short name=GDH EC=1.4.1.3 | ||
| Gene names |
| ||
| Organism | Pyrococcus endeavori | ||
| Taxonomic identifier | 39456 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 420 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H. |
| Subunit structure | Homohexamer. |
| Subcellular location | CytoplasmBy similarity. |
| Sequence similarities | Belongs to the Glu/Leu/Phe/Val dehydrogenases family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | amino acid metabolic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro glutamate dehydrogenase [NAD(P)+] activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Characterization, cloning, and in vitro expression of the extremely thermostable glutamate dehydrogenase from the hyperthermophilic Archaeon, ES4." Diruggiero J., Robb F.T., Jagus R., Klump H.H., Borges K.M., Kessel M., Mai X., Adams M.W.W.A. J. Biol. Chem. 268:17767-17774(1993) [PubMed: 8349661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION. Strain: ES4. |
Cross-references
Sequence databases | |
|---|---|
| L12408 Genomic DNA. Translation: AAA64795.1. | |
| PIR | A47410. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GTM based on UniProtKB P80319. |
| SMR | Q47951. Positions 5-420. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR006095. Glu/Leu/Phe/Val_DHase. IPR006096. Glu/Leu/Phe/Val_DHase_C. IPR006097. Glu/Leu/Phe/Val_DHase_dimer. IPR014362. Glu_DHase. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR11606:SF2. GLFV_DH. 1 hit. |
| Pfam | PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000185. Glu_DH. 1 hit. |
| PRINTS | PR00082. GLFDHDRGNASE. |
| PROSITE | PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHE3_PYREN | ||||||||
| Accession | Primary (citable) accession number: Q47951 | ||||||||
| 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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