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Q56304 (DHE3_THELI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate dehydrogenase

Short name=GDH
EC=1.4.1.3
Gene names
Name:gdhA
OrganismThermococcus litoralis
Taxonomic identifier2265 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.

Subunit structure

Homohexamer. Ref.3

Subcellular location

Cytoplasm Ref.2.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is above 95 degrees Celsius.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 419418Glutamate dehydrogenase
PRO_0000182762

Regions

Nucleotide binding219 – 2257NAD Potential

Sites

Active site1051 By similarity

Secondary structure

.................................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56304 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2768747A590B71F6

FASTA41946,740
        10         20         30         40         50         60 
MVEQDPFEIA VKQLERAAQY MDISEEALEF LKRPQRIVEV SIPVEMDDGS VKVFTGFRVQ 

        70         80         90        100        110        120 
YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGVIC NPKEMSDREK 

       130        140        150        160        170        180 
ERLARGYVRA IYDVISPYTD IPAPDVYTNP QIMAWMMDEY ETISRRKDPS FGVITGKPPS 

       190        200        210        220        230        240 
VGGIVARMDA TARGASYTVR EAAKALGMDL KGKTIAIQGY GNAGYYMAKI MSEEYGMKVV 

       250        260        270        280        290        300 
AVSDTKGGIY NPDGLNADEV LAWKKKTGSV KDFPGATNIT NEELLELEVD VLAPSAIEEV 

       310        320        330        340        350        360 
ITKKNADNIK AKIVAELANG PTTPEADEIL YEKGILIIPD FLCNAGGVTV SYFEWVQNIT 

       370        380        390        400        410 
GDYWTVEETR AKLDKKMTKA FWDVYNTHKE KNINMRDAAY VVAVSRVYQA MKDRGWIKK 

« Hide

References

[1]"Cloning and sequencing of glutamate dehydrogenases from hyperthermophilic archaea."
Borges K.M., Diruggiero J., Robb F.T.
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis."
Ma K., Robb F.T., Adams M.W.W.
Appl. Environ. Microbiol. 60:562-568(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, SUBCELLULAR LOCATION.
Strain: DSM 5473.
[3]"Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus."
Britton K.L., Yip K.S.P., Sedelnikova S.E., Stillman T.J., Adams M.W.W., Ma K., Maeder D.L., Robb F.T., Tolliday N., Vetriani C., Rice D.W., Baker P.J.
J. Mol. Biol. 293:1121-1132(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19995 Genomic DNA. Translation: AAA72393.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVUX-ray2.50A/B/C/D/E/F2-419[»]
ProteinModelPortalQ56304.
SMRQ56304. Positions 4-419.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFPIRSF000185. Glu_DH. 1 hit.
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ56304.

Entry information

Entry nameDHE3_THELI
AccessionPrimary (citable) accession number: Q56304
Secondary accession number(s): Q9UWK7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references