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InterPro: IPR019818 Isocitrate/isopropylmalate dehydrogenase, conserved site
Protein matches
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UniProtKB Matches: 4196 proteins |
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Accession
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IPR019818 IsoCit/isopropylmalate_DH_CS |
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Type
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Conserved_site |
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Signatures
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InterPro Relationships
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Found in
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IPR001804 Isocitrate/isopropylmalate dehydrogenase
IPR004429 Isopropylmalate dehydrogenase
IPR004434 Isocitrate dehydrogenase NAD-dependent, mitochondrial
IPR004439 Isocitrate dehydrogenase NADP-dependent, prokaryotic
IPR004790 Isocitrate dehydrogenase NADP-dependent, eukaryotic
IPR011828 Isopropylmalate/isohomocitrate dehydrogenase
IPR011829 Tartrate dehydrogenase
IPR014273 Isocitrate dehydrogenase bacteria
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GO Term annotation
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Process
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GO:0055114 oxidation reduction
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Function
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GO:0000287 magnesium ion binding
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD or NADH binding
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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Isocitrate dehydrogenase (IDH) [1, 2] is an important enzyme of carbohydrate metabolism which catalyses 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.
3-isopropylmalate dehydrogenase (EC:1.1.1.85) (IMDH) [3, 4] catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate. Tartrate dehydrogenase (EC:1.1.1.93) [5] catalyses the reduction of tartrate to oxaloglycolate.
These enzymes are evolutionary related [1, 3, 4, 5]. The signature pattern of this entry is located in a conserved region, which contains a glycine-rich stretch of residues located in the C-terminal section.
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Structural links
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Database links
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Publications
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1.
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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
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2.
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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
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3.
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Imada K, Sato M, Tanaka N, Katsube Y, Matsuura Y, Oshima T.
Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution.
J. Mol. Biol. 222 725-38 1991
[PubMed: 1748999]
http://dx.doi.org/10.1016/0022-2836(91)90508-4
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4.
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Zhang T, Koshland DE Jr.
Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase.
Protein Sci. 4 84-92 1995
[PubMed: 7773180]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7773180
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5.
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Tipton PA, Beecher BS.
Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases.
Arch. Biochem. Biophys. 313 15-21 1994
[PubMed: 8053675]
http://dx.doi.org/10.1006/abbi.1994.1352
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Additional Reading
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Taylor AB, Hu G, Hart PJ, McAlister-Henn L.
Allosteric motions in structures of yeast NAD+-specific isocitrate dehydrogenase.
J. Biol. Chem. 283 2008 10872-80
[PubMed: 18256028]
http://dx.doi.org/10.1074/jbc.M708719200
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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
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Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS.
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.
Acta Crystallogr. D Biol. Crystallogr. 63 2007 366-80
[PubMed: 17327674]
http://dx.doi.org/10.1107/S0907444906055624
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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
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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
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InterPro 23.1
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