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Reviewed, UniProtKB/Swiss-Prot Q47950 (DHE3_PYRAB)

Last modified November 25, 2008. Version 58. 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

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Names and origin

Protein namesRecommended name:
    Glutamate dehydrogenase
      Short name=GDH
    EC=1.4.1.3
Gene names
Name: gdhA
Synonyms: gdh
Ordered Locus Names: PYRAB05690
ORF Names: PAB0391
OrganismPyrococcus abyssi [Complete proteome] [HAMAP]
Taxonomic identifier29292 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

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Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H.

Subunit structure

Homohexamer By similarity.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

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

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Ontologies

Keywords

   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome

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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Glutamate dehydrogenase
PRO_0000182755

Regions

Nucleotide binding220 – 2267NAD Potential

Sites

Active site1051 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q47950-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 82F8B343572DFE2B

FASTA42047,098
        10         20         30         40         50         60 
MVEQDPFEIA VKQLERAAQY MKISEEALEF LKRPQRIVEV TIPVEMDDGS VKVFTGFRVQ 

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

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

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

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

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

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

« Hide

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References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"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] OF 22-255.
Strain: GE5 / Orsay.

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Cross-references

Sequence databases

AJ248284 Genomic DNA. Translation: CAB49491.1.
L19116 Genomic DNA. Translation: AAA64796.1.
PIRD75176.
RefSeqNP_126260.1.

3D structure databases

HSSPHSSP built from PDB template 1GTM based on UniProtKB P80319.
SMRQ47950. Positions 5-420.
ModBaseSearch...

Genome annotation databases

GeneID1495474.
GenomeReviewsGene locus PYRAB05690 in contig AL096836_GR.
KEGGpab:PAB0391.
NMPDRfig|272844.1.peg.598.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ47950.

Enzyme and pathway databases

BioCycPABY272844:PAB0391-MON.

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...

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Entry information

Entry nameDHE3_PYRAB
AccessionPrimary (citable) accession number: Q47950
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 25, 2008
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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