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Reviewed, UniProtKB/Swiss-Prot Q56304 (DHE3_THELI)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 processamino acid metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glutamate dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: 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
Q56304-1 [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: 8135516] [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: 10547290] [Abstract]
Cited for: SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

L19995 Genomic DNA. Translation: AAA72393.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BVUX-ray2.50A/B/C/D/E/F2-419[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.4.1.3. 74708.

Family and domain databases

InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11606:SF2. GLFV_DH. 1 hit.
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFPIRSF000185. Glu_DH. 1 hit.
PRINTSPR00082. GLFDHDRGNASE.
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 59 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents