{PDOC00979}
{PS01272; GCKR}
{BEGIN}
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* Glucokinase regulatory protein family signature *
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The  glucokinase  regulatory  protein  (GCKR) [1] is a vertebrate protein that
inhibits  glucokinase by forming a complex with the enzyme, which plays a role
in  the control of blood glucose homeostasis. GCKR is a protein of about 70 Kd
which  is  evolutionary  related to bacterial N-acetylmuramic acid 6-phosphate
etherases  (MurNAc-6-P  etherase,  murQ) which are about half the size of GCKR
and  form active homodimers. MurNAc-6-P etherases catalyze the cleavage of the
D-lactyl  ether substituent of the bacterial cell wall sugar MurNAc and play a
role  in  recycling  of the cell wall [2]. The 3D structure of the Haemophilus
influenzae HI0754/murQ protein (see <PDB:1NRI>) shows structural relationships
with  other  sugar  isomerase  (SIS)  domain  proteins  (see  <PDOC51464>). In
contrast to mono-SIS bacterial MurNAc-6-P etherase, mammalian GCKR is composed
of two SIS domains.

As a  signature  pattern,  we  selected  one  of  at least four well conserved
regions found in those proteins.

-Consensus pattern: G-[PA]-E-x-[LIV]-[STAM]-G-S-[ST]-R-[LIVM]-K-[STGA](3)-
                    x(2)-K
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2009 / Text revised.

[ 1] Veiga-Da-Cunha M., Detheux M., Watelet N., Van Schaftingen E.
     "Cloning and expression of a Xenopus liver cDNA encoding a
     fructose-phosphate-insensitive regulatory protein of glucokinase."
     Eur. J. Biochem. 225:43-51(1994).
     PubMed=7925465;
[ 2] Jaeger T., Mayer C.
     "N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in
     cell wall metabolism, distribution, structure, and mechanism."
     Cell. Mol. Life Sci. 65:928-939(2008).
     PubMed=18049859; DOI=10.1007/s00018-007-7399-

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