{PDOC00389}
{PS00470; IDH_IMDH}
{BEGIN}
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* Isocitrate and isopropylmalate dehydrogenases signature *
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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.

3-isopropylmalate dehydrogenase (EC 1.1.1.85) (IMDH) [3,4] catalyzes 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] catalyzes the reduction of tartrate
to oxaloglycolate.

These enzymes are evolutionary related [1,3,4,5]. The best conserved region of
these enzymes is  a glycine-rich stretch of residues located in the C-terminal
section. We have used this region as a signature pattern.

-Consensus pattern: [NSK]-[LIMYTV]-[FYDNH]-[GEA]-[DNGSTY]-[IMVYL]-x-[STGDN]-
                    [DN]-x(1,2)-[SGAP]-x(3,4)-[GE]-[STG]-[LIVMPA]-[GA]-[LIVMF]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2004 / Pattern and text revised.

[ 1] Hurley J.H., Thorsness P.E., Ramalingam V., Helmers N.H.,
     Koshland D.E. Jr., Stroud R.M.
     "Structure of a bacterial enzyme regulated by phosphorylation,
     isocitrate dehydrogenase."
     Proc. Natl. Acad. Sci. U.S.A. 86:8635-8639(1989).
     PubMed=2682654
[ 2] Cupp J.R., McAlister-Henn L.
     "NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide
     sequence, and disruption of the IDH2 gene from Saccharomyces
     cerevisiae."
     J. Biol. Chem. 266:22199-22205(1991).
     PubMed=1939242
[ 3] 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. 222:725-738(1991).
     PubMed=1748999
[ 4] Zhang T., Koshland D.E. Jr.
     "Modeling substrate binding in Thermus thermophilus isopropylmalate
     dehydrogenase."
     Protein Sci. 4:84-92(1995).
     PubMed=7773180
[ 5] Tipton P.A., Beecher B.S.
     "Tartrate dehydrogenase, a new member of the family of metal-dependent
     decarboxylating R-hydroxyacid dehydrogenases."
     Arch. Biochem. Biophys. 313:15-21(1994).
     PubMed=8053675

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