{PDOC00114}
{PS00124; FBPASE}
{BEGIN}
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* Fructose-1-6-bisphosphatase active site *
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Fructose-1,6-bisphosphatase (EC 3.1.3.11) (FBPase) [1], a regulatory enzyme in
gluconeogenesis,  catalyzes  the  hydrolysis  of  fructose 1,6-bisphosphate to
fructose 6-phosphate.  It is involved in many different metabolic pathways and
found in most organisms.

Sedoheptulose-1,7-bisphosphatase (EC 3.1.3.37) (SBPase) [2] is an enzyme found
plant chloroplast and in photosynthetic bacteria that catalyzes the hydrolysis
of sedoheptulose  1,7-bisphosphate to sedoheptulose 7-phosphate, a step in the
Calvin's reductive   pentose   phosphate   cycle.   It   is  functionally  and
structurally related to FBPase.

In mammalian FBPase, a lysine residue has  been shown  to  be  involved in the
catalytic mechanism [3].  The  region  around this residue is highly conserved
and can be used as a signature pattern for FBPase and SBPase. It must be noted
that, in  some  bacterial FBPase sequences, the active site lysine is replaced
by an arginine.

-Consensus pattern: [AG]-[RK]-[LI]-x(1,2)-[LIV]-[FY]-E-x(2)-P-[LIVM]-[GSA]
                    [K/R is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2001 / Pattern and text revised.

[ 1] Benkovic S.J., DeMaine M.M.
     "Mechanism of action of fructose 1,6-bisphosphatase."
     Adv. Enzymol. 53:45-82(1982).
     PubMed=6277165
[ 2] Raines C.A., Lloyd J.C., Willingham N.M., Potts S., Dyer T.A.
     "cDNA and gene sequences of wheat chloroplast
     sedoheptulose-1,7-bisphosphatase reveal homology with
     fructose-1,6-bisphosphatases."
     Eur. J. Biochem. 205:1053-1059(1992).
     PubMed=1374332
[ 3] Ke H.M., Thorpe C.M., Seaton B., Lipscomb W.N., Marcus F.
     "Structure refinement of fructose-1,6-bisphosphatase and its fructose
     2,6-bisphosphate complex at 2.8 A resolution."
     J. Mol. Biol. 212:513-539(1990).
     PubMed=2157849

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