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P96110 (DHE3_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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:TM_1015
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homohexamer.

Sequence similarities

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

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 75 degrees Celsius. Thermostable.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 416415Glutamate dehydrogenase
PRO_0000182764

Sites

Active site1051

Experimental info

Sequence conflict1531M → I in CAA71058. Ref.1

Secondary structure

........................................................................ 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P96110 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: D7294929879CB4F2

FASTA41645,821
        10         20         30         40         50         60 
MPEKSLYEMA VEQFNRAASL MDLESDLAEV LRRPKRVLIV EFPVRMDDGH VEVFTGYRVQ 

        70         80         90        100        110        120 
HNVARGPAKG GIRYHPDVTL DEVKALAFWM TWKTAVMNLP FGGGKGGVRV DPKKLSRNEL 

       130        140        150        160        170        180 
ERLSRRFFSE IQVIIGPYND IPAPDVNTNA DVMAWYMDTY SMNVGHTVLG IVTGKPVELG 

       190        200        210        220        230        240 
GSKGREEATG RGVKVCAGLA MDVLGIDPKK ATVAVQGFGN VGQFAALLIS QELGSKVVAV 

       250        260        270        280        290        300 
SDSRGGIYNP EGFDVEELIR YKKEHGTVVT YPKGERITNE ELLELDVDIL VPAALEGAIH 

       310        320        330        340        350        360 
AGNAERIKAK AVVEGANGPT TPEADEILSR RGILVVPDIL ANAGGVTVSY FEWVQDLQSF 

       370        380        390        400        410 
FWDLDQVRNA LEKMMKGAFN DVMKVKEKYN VDMRTAAYIL AIDRVAYATK KRGIYP 

« Hide

References

« Hide 'large scale' references
[1]"Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: molecular characterization and phylogenetic implications."
Kort R., Liebl W., Labedan B., Forterre P., Eggen R.I.L., de Vos W.M.
Extremophiles 1:52-60(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, CHARACTERIZATION.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0-A resolution."
Knapp S., de Vos W.M., Rice D., Ladenstein R.
J. Mol. Biol. 267:916-932(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[4]"Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region."
Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M.
J. Mol. Biol. 280:287-296(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
[5]"Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface."
Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M.
J. Mol. Biol. 289:357-369(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09925 Genomic DNA. Translation: CAA71058.1.
AE000512 Genomic DNA. Translation: AAD36092.1.
PIRG72305.
T45284.
RefSeqNP_228821.1. NC_000853.1.
YP_007977367.1. NC_021214.1.
YP_008991888.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B26X-ray3.00A/B/C/D/E/F1-416[»]
1B3BX-ray3.10A/B/C/D/E/F2-416[»]
2TMGX-ray2.90A/B/C/D/E/F2-416[»]
ProteinModelPortalP96110.
SMRP96110. Positions 5-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36092; AAD36092; TM_1015.
GeneID896847.
KEGGtma:TM1015.
tmi:THEMA_09280.
tmm:Tmari_1018.
PATRIC23936959. VBITheMar51294_1028.

Phylogenomic databases

eggNOGCOG0334.
KOK00261.
OMATMELCQK.
OrthoDBEOG65XN4D.

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-4406-MONOMER.

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

EvolutionaryTraceP96110.

Entry information

Entry nameDHE3_THEMA
AccessionPrimary (citable) accession number: P96110
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 104 of the entry and version 4 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