The domain within your query sequence starts at position 6 and ends at position 71; the E-value for the Iso_dh domain shown below is 1.8e-15.



PFAM accession number:PF00180
Interpro abstract (IPR024084):

The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate dehydrogenase.

IDH is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate [(PUBMED:2682654), (PUBMED:1939242)]. IDH is either dependent on NAD+ (EC or on NADP+ (EC 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.

IMDH (EC catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate [(PUBMED:1748999), (PUBMED:7773180)].

Tartrate dehydrogenase (EC shows strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase [(PUBMED:8053675)]. It catalyses the reduction of tartrate to oxaloglycolate [(PUBMED:8053675)].

This entry represents a structural domain found in all types of isocitrate dehydrogenase, and in isopropylmalate dehydrogenase and tartrate dehydrogenase. The crystal structure of Escherichia coli isopropylmalate dehydrogenase has been described [(PUBMED:9086278)].

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Iso_dh