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InterPro: IPR004790 Isocitrate dehydrogenase NADP-dependent, eukaryotic

Protein matches Help

UniProtKB

Matches:

868 proteins

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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

IPR004790 Isocitrate_DH_NADP-dep_euk

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000108	IDH_NADP	628
PANTHER	PTHR11822	IDH_NADP_euk	860
TIGRFAMs	TIGR00127	nadp_idh_euk	709
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001804 Isocitrate/isopropylmalate dehydrogenase

Contains

IPR019818 Isocitrate/isopropylmalate dehydrogenase, conserved site

GO Term annotation Help

Process

GO:0006102 isocitrate metabolic process
GO:0055114 oxidation reduction

Function

GO:0004450 isocitrate dehydrogenase (NADP+) activity

InterPro annotation

Entry Details in BioMart

Abstract

Isocitrate dehydrogenase (IDH) [1, 2] is an important enzyme of carbohydrate metabolism which catalyzes the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. IDH is either dependent on NAD⁺ (EC:1.1.1.41) or on NADP⁺ (EC:1.1.1.42). In eukaryotes there are at least three isozymes of IDH: two are located in the mitochondrial matrix (one NAD⁺-dependent, the other NADP⁺-dependent), while the third one (also NADP⁺-dependent) is cytoplasmic. In Escherichia coli the activity of a NADP⁺-dependent form of the enzyme is controlled by the phosphorylation of a serine residue; the phosphorylated form of IDH is completely inactivated.

The eukaryotic, NADP-dependent isocitrate dehydrogenases, are defined by this group that includes the cytosolic, mitochondrial, and chloroplast enzymes, but does also hit a small number of bacterial proteins.

Structural links Help

PDB - click here

SCOP: c.77.1.1

CATH: 3.40.718.10

Database links Help

Enzyme: EC:1.1.1.42

CluSTr: ALLvsALL:2083:40.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004790

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O75874 Isocitrate dehydrogenase [NADP] cytoplasmic

O88844 Isocitrate dehydrogenase [NADP] cytoplasmic

P21954 Isocitrate dehydrogenase [NADP], mitochondrial

P41562 Isocitrate dehydrogenase [NADP] cytoplasmic

P50215 Isocitrate dehydrogenase [NADP]

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR019818	Isocitrate/isopropylmalate dehydrogenase, conserved site
IPR001804	Isocitrate/isopropylmalate dehydrogenase
IPR004790	Isocitrate dehydrogenase NADP-dependent, eukaryotic
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM. Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 86 8635-9 1989 [PubMed: 2682654] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2682654
2.	Cupp JR, McAlister-Henn L. NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae. J. Biol. Chem. 266 22199-205 1991 [PubMed: 1939242] http://intl.jbc.org/cgi/content/abstract/266/33/22199

Additional Reading Open in usermanual
	Karlstrom M, Steen IH, Madern D, Fedoy AE, Birkeland NK, Ladenstein R. The crystal structure of a hyperthermostable subfamily II isocitrate dehydrogenase from Thermotoga maritima. FEBS J. 273 2006 2851-68 [PubMed: 16759231] http://dx.doi.org/10.1111/j.1742-4658.2006.05298.x
	Fedoy AE, Yang N, Martinez A, Leiros HK, Steen IH. Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability. J. Mol. Biol. 372 2007 130-49 [PubMed: 17632124] http://dx.doi.org/10.1016/j.jmb.2007.06.040
	Xu X, Zhao J, Xu Z, Peng B, Huang Q, Arnold E, Ding J. Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J. Biol. Chem. 279 2004 33946-57 [PubMed: 15173171] http://dx.doi.org/10.1074/jbc.M404298200
	Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ. Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism. J. Biol. Chem. 277 2002 43454-62 [PubMed: 12207025] http://dx.doi.org/10.1074/jbc.M207306200

InterPro 23.1