{PDOC00638}
{PS00808; ADP_GLC_PYROPHOSPH_1}
{PS00809; ADP_GLC_PYROPHOSPH_2}
{PS00810; ADP_GLC_PYROPHOSPH_3}
{BEGIN}
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* ADP-glucose pyrophosphorylase signatures *
********************************************

ADP-glucose  pyrophosphorylase (glucose-1-phosphate adenylyltransferase) [1,2]
(EC 2.7.7.27)  catalyzes  a  very  important  step   in  the  biosynthesis  of
alpha 1,4-glucans  (glycogen  or  starch) in bacteria and plants: synthesis of
the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP.

ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme.
It is a homotetramer in bacteria while in plant  chloroplasts and amyloplasts,
it is a heterotetramer of two different, yet evolutionary related, subunits.

There are a number of  conserved  regions in  the  sequence  of  bacterial and
plant ADP-glucose  pyrophosphorylase  subunits.  We  selected  three  of these
regions as  signature  patterns.  The  first  two are N-terminal and have been
proposed to  be  part  of the allosteric and/or substrate-binding sites in the
Escherichia coli  enzyme  (gene  glgC).  The  third  pattern  corresponds to a
conserved region in the central part of the enzymes.

-Consensus pattern: [AG]-G-G-x-G-[STKA]-x-L-x(2)-L-[TA]-x(3)-[AST]-x-P-[AS]-
                    [LV]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: W-[FY]-x-G-[ST]-[AS]-[DNSH]-[AS]-[LIVMFYW]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [APV]-[GS]-M-G-[LIVMN]-Y-[IVC]-[LIVMFY]-x(2)-[DENPHKRQS]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2004 / Patterns and text revised.

[ 1] Nakata P.A., Greene T.W., Anderson J.M., Smith-White B.J., Okita T.W.,
     Preiss J.
     "Comparison of the primary sequences of two potato tuber ADP-glucose
     pyrophosphorylase subunits."
     Plant Mol. Biol. 17:1089-1093(1991).
     PubMed=1657244;
[ 2] Preiss J., Ball K., Hutney J., Smith-White B.J., Li. L., Okitsa T.W.
     Pure Appl. Chem. 63:535-544(1991).

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