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Reviewed, UniProtKB/Swiss-Prot O74024 (DHE3_THEPR)

Last modified June 16, 2009. Version 50. 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
OrganismThermococcus profundus
Taxonomic identifier49899 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

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Protein attributes

Sequence length419 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 By similarity.

Sequence similarities

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

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Ontologies

Keywords
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processamino acid metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

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 – 419419Glutamate dehydrogenase
PRO_0000182763

Regions

Nucleotide binding219 – 2257NAD Potential

Sites

Active site1051 By similarity

Secondary structure

1 ................................................................... 419
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O74024-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 1DF3C1122E562706

FASTA41946,700
        10         20         30         40         50         60 
MVEIDPFEMA VKQLERAAQY MDISEEALEW LKKPMRIVEV SVPIEMDDGS VKVFTGFRVQ 

        70         80         90        100        110        120 
HNWARGPTKG GIRWHPAETL STVKALATWM TWKVAVVDLP YGGGKGGIIV NPKELSEREQ 

       130        140        150        160        170        180 
ERLARAYIRA VYDVIGPWTD IPAPDVYTNP KIMGWMMDEY ETIMRRKGPA FGVITGKPLS 

       190        200        210        220        230        240 
IGGSLGRGTA TAQGAIFTIR EAAKALGIDL KGKKIAVQGY GNAGYYTAKL AKEQLGMTVV 

       250        260        270        280        290        300 
AVSDSRGGIY NPDGLDPDEV LKWKREHGSV KDFPGATNIT NEELLELEVD VLAPAAIEEV 

       310        320        330        340        350        360 
ITEKNADNIK AKIVAEVANG PVTPEADDIL REKGILQIPD FLCNAGGVTV SYFEWVQNIN 

       370        380        390        400        410 
GYYWTEEEVR EKLDKKMTKA FWEVYNTHKD KNIHMRDAAY VVAVSRVYQA MKDRGWVKK

« Hide

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References

[1]"Molecular cloning, nucleotide sequence and expression in Escherichia coli of hyperthermophilic glutamate dehydrogenase gene from Thermococcus profundus."
Higuchi S., Kobayashi T., Kimura K., Horikoshi K., Kudo T.
J. Ferment. Bioeng. 83:405-411(1997)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

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Cross-references

Sequence databases

D87814 Genomic DNA. Translation: BAA28943.1.
PIRT44308.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EUZX-ray2.25A/B/C/D/E/F1-419[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.4.1.3. 256746.

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_THEPR
AccessionPrimary (citable) accession number: O74024
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 50 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)

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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