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Reviewed, UniProtKB/Swiss-Prot Q47951 (DHE3_PYREN)

Last modified November 25, 2008. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismPyrococcus endeavori
Taxonomic identifier39456 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termDirect 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-KW

   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

Chain1 – 420420Glutamate dehydrogenase
PRO_0000182756

Regions

Nucleotide binding220 – 2267NAD Potential

Sites

Active site1051 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47951-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 26C571CC5DEF85CB

FASTA42047,141
        10         20         30         40         50         60 
MVEQDPFEIA VKQLERAAQY MKISEEALEF LKRPQRIVEV TIPVEMDDGT VKVFTGFRVQ 

        70         80         90        100        110        120 
YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGIIV DPKKLSDREK 

       130        140        150        160        170        180 
ERLARGYIRA IYDVISPYED IPAPDVYTNP QIMAWMMDEY EAISRRKTPA FGIITGKPLS 

       190        200        210        220        230        240 
IGGSLGRNEA TARGASYTIR EARKVLGWGD LKGKTIAIQG YGNAGYYLAK IMSEDYGMKV 

       250        260        270        280        290        300 
VAVSDSKGGI YNPDGLNADE VLKWKQEHGS VKDFPGATNI TNEELLELEV DVLAPAAIEE 

       310        320        330        340        350        360 
VITKKNADNI KAKIVAEVAN GPVTPEADEI LFEKGILQIP DFLCNAGGVT VSYFEWVQNI 

       370        380        390        400        410        420 
TGYYWTLEEV REKLDKKMTK AFYDVYNTAK EKNIHMRDAD YVVAVQRVYQ AMLDRGWVKH 

« Hide

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.
PIRA47410.

3D structure databases

HSSPHSSP built from PDB template 1GTM based on UniProtKB P80319.
SMRQ47951. Positions 5-420.
ModBaseSearch...

Family and domain databases

InterProIPR006095. 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]
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_PYREN
AccessionPrimary (citable) accession number: Q47951
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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