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P80319 (DHE3_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. 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
Synonyms:gdh
Ordered Locus Names:PF1602
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
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

Chain1 – 420420Glutamate dehydrogenase
PRO_0000182757

Regions

Nucleotide binding220 – 2267NAD Potential

Sites

Active site1051

Experimental info

Sequence conflict88 – 892AW → WA AA sequence Ref.2
Sequence conflict3661T → K AA sequence Ref.2

Secondary structure

..................................................................... 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80319 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 673DB20F8764A93C

FASTA42047,114
        10         20         30         40         50         60 
MVEQDPYEIV IKQLERAAQY MEISEEALEF LKRPQRIVEV TIPVEMDDGS VKVFTGFRVQ 

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

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

       190        200        210        220        230        240 
IGGSLGRIEA TARGASYTIR EAAKVLGWDT LKGKTIAIQG YGNAGYYLAK IMSEDFGMKV 

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

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

       370        380        390        400        410        420 
TGYYWTIEEV RERLDKKMTK AFYDVYNIAK EKNIHMRDAA YVVAVQRVYQ AMLDRGWVKH 

« Hide

References

« Hide 'large scale' references
[1]"The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence."
Eggen R.I.L., Geerling A.C.M., Waldkoetter K., Antranikian G., de Vos W.M.
Gene 132:143-148(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium."
Maras B., Valiante S., Chiaraluce R., Consalvi V., Politi L., de Rosa M., Bossa F., Scandurra R., Barra D.
J. Protein Chem. 13:253-259(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[4]"The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures."
Yip K.S.P., Stillman T.J., Britton K.L., Artymiuk P.J., Baker P.J., Sedelnikova S.E., Engel P.C., Pasquo A., Chiaraluce R., Consalvi V., Scandurra R., Rice D.W.
Structure 3:1147-1158(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97860 Genomic DNA. Translation: AAA83390.1.
AE009950 Genomic DNA. Translation: AAL81726.1.
PIRJN0854. T46971.
RefSeqNP_579331.1. NC_003413.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTMX-ray2.20A/B/C2-420[»]
ProteinModelPortalP80319.
SMRP80319. Positions 5-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1602.

Proteomic databases

PRIDEP80319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81726; AAL81726; PF1602.
GeneID1469478.
KEGGpfu:PF1602.

Phylogenomic databases

eggNOGCOG0334.
HOGENOMHOG000243801.
KOK00261.
OMAFNFDRAK.

Enzyme and pathway databases

SABIO-RKP80319.

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

EvolutionaryTraceP80319.

Entry information

Entry nameDHE3_PYRFU
AccessionPrimary (citable) accession number: P80319
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 102 of the entry and version 2 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