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.
FAQAVGRNIANPTAMLLSATNMLRHLNLEYHSSMIADAVKKVIKAGKVRTRDMGGYSTTT DFIKSV
Iso_dh |
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| PFAM accession number: | PF00180 |
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| Interpro abstract (IPR024084): | 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) ]. 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 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. IMDH ( EC 1.1.1.85 ) 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 1.1.1.93 ) 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) ]. |
| 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