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Reviewed, UniProtKB/Swiss-Prot P80319 (DHE3_PYRFU)

Last modified June 16, 2009. Version 73. 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

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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: PF1602
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [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 existenceEvidence at protein level.

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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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
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...

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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

1 ..................................................................... 420
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P80319-1 [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

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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: 8406037] [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: 8060497] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
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: 8591026] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

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Cross-references

Sequence databases

M97860 Genomic DNA. Translation: AAA83390.1.
AE010260 Genomic DNA. Translation: AAL81726.1.
PIRJN0854. T46971.
RefSeqNP_579331.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GTMX-ray2.20A/B/C2-420[»]
ModBaseSearch...

Genome annotation databases

GeneID1469478.
GenomeReviewsGene locus PF1602 in contig AE009950_GR.
KEGGpfu:PF1602.
NMPDRfig|186497.1.peg.1649.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP80319.
OMAP80319. YLAKIMS.

Enzyme and pathway databases

BRENDA1.4.1.3. 321.

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...

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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: June 16, 2009
This is version 73 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

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