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InterPro: IPR014362 Glutamate dehydrogenase

Protein matches Help

UniProtKB

Matches:

1731 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR014362 Glu_DH

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000185	Glu_DH	1731
Signatures in BioMart

InterPro Relationships Help

Parent

IPR006095 Glutamate/phenylalanine/leucine/valine dehydrogenase

Contains

IPR006096 Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
IPR006097 Glutamate/phenylalanine/leucine/valine dehydrogenase, dimerisation domain

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016639 oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a glutamate dehydrogenase.

Structural links Help

PDB - click here

SCOP: c.2.1.7 , c.58.1.1

CATH: 1.10.285.10 , 3.40.192.10 , 3.40.50.720

Database links Help

Enzyme: EC:1.4.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR014362

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00368 Glutamate dehydrogenase 1, mitochondrial

P07262 NADP-specific glutamate dehydrogenase 1

P24295 NAD-specific glutamate dehydrogenase

P54386 NADP-specific glutamate dehydrogenase

Q38946 Glutamate dehydrogenase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016040	NAD(P)-binding domain
IPR006095	Glutamate/phenylalanine/leucine/valine dehydrogenase
IPR006097	Glutamate/phenylalanine/leucine/valine dehydrogenase, dimerisation domain
IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
IPR014362	Glutamate dehydrogenase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Nakasako M, Fujisawa T, Adachi S, Kudo T, Higuchi S. Large-scale domain movements and hydration structure changes in the active-site cleft of unligated glutamate dehydrogenase from Thermococcus profundus studied by cryogenic X-ray crystal structure analysis and small-angle X-ray scattering. Biochemistry 40 2001 3069-79 [PubMed: 11258921] http://dx.doi.org/10.1021/bi002482x
	Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H. The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. J. Mol. Biol. 345 2005 325-37 [PubMed: 15571725] http://dx.doi.org/10.1016/j.jmb.2004.10.063
	Stillman TJ, Migueis AM, Wang XG, Baker PJ, Britton KL, Engel PC, Rice DW. Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum. J. Mol. Biol. 285 1999 875-85 [PubMed: 9878450] http://dx.doi.org/10.1006/jmbi.1998.2335
	Lebbink JH, Knapp S, van der Oost J, Rice D, Ladenstein R, de Vos WM. Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface. J. Mol. Biol. 289 1999 357-69 [PubMed: 10366510] http://dx.doi.org/10.1006/jmbi.1999.2779
	Britton KL, Yip KS, Sedelnikova SE, Stillman TJ, Adams MW, Ma K, Maeder DL, Robb FT, Tolliday N, Vetriani C, Rice DW, Baker PJ. Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus. J. Mol. Biol. 293 1999 1121-32 [PubMed: 10547290] http://dx.doi.org/10.1006/jmbi.1999.3205

InterPro 23.1