EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR004439 Isocitrate dehydrogenase NADP-dependent, prokaryotic

Protein matches Help

UniProtKB

Matches:

959 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

IPR004439 Isocitrate_DH_NADP_prok

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR11835:SF1	NADP_IDH_prok	770
TIGRFAMs	TIGR00183	prok_nadp_idh	745
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001804 Isocitrate/isopropylmalate dehydrogenase

Contains

IPR019818 Isocitrate/isopropylmalate dehydrogenase, conserved site

GO Term annotation Help

Process

GO:0006099 tricarboxylic acid cycle
GO:0055114 oxidation reduction

Function

GO:0004450 isocitrate dehydrogenase (NADP+) activity

InterPro annotation

Entry Details in BioMart

Abstract

Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the multimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; the latter carbon, now adjacent to a carbonyl group, readily decarboxylates.

Prokaryotic NADP-dependent isocitrate dehydrogenases (EC:1.1.1.42) resemble their NAD-dependent counterparts and 3-isopropylmalate dehydrogenase (an NAD-dependent enzyme) more closely than they resemble eukaryotic NADP-dependent isocitrate dehydrogenases.

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:57597:95.2

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004439

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O29610 Isocitrate dehydrogenase [NADP]

P08200 Isocitrate dehydrogenase [NADP]

P50214 Isocitrate dehydrogenase [NADP]

P80046 Isocitrate dehydrogenase [NADP]

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004439	Isocitrate dehydrogenase NADP-dependent, prokaryotic
IPR019818	Isocitrate/isopropylmalate dehydrogenase, conserved site
IPR001804	Isocitrate/isopropylmalate dehydrogenase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Imada K, Tamura T, Takenaka R, Kobayashi I, Namba K, Inagaki K. Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity. Proteins 70 2008 63-71 [PubMed: 17634983] http://dx.doi.org/10.1002/prot.21486
	Jeong JJ, Sonoda T, Fushinobu S, Shoun H, Wakagi T. Crystal structure of isocitrate dehydrogenase from Aeropyrum pernix. Proteins 55 2004 1087-9 [PubMed: 15146507] http://dx.doi.org/10.1002/prot.20121
	Doyle SA, Beernink PT, Koshland DE Jr. Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP. Biochemistry 40 2001 4234-41 [PubMed: 11284679] http://dx.doi.org/10.1021/bi002533q
	Stokke R, Karlstrom M, Yang N, Leiros I, Ladenstein R, Birkeland NK, Steen IH. Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers. Extremophiles 11 2007 481-93 [PubMed: 17401542] http://dx.doi.org/10.1007/s00792-006-0060-z
	Karlstrom M, Stokke R, Steen IH, Birkeland NK, Ladenstein R. Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability. J. Mol. Biol. 345 2005 559-77 [PubMed: 15581899] http://dx.doi.org/10.1016/j.jmb.2004.10.025

InterPro 23.1