{PDOC01037}
{PS01335; METHYLGLYOXAL_SYNTH}
{BEGIN}
**************************************
* Methylglyoxal synthase active site *
**************************************

Methylglyoxal synthase  (EC  4.2.3.3) (MGS) [1]  catalyzes  the  conversion of
dihydroxyacetone phosphate   to   methylglyoxal  and  phosphate.  It  provides
bacteria with  an  alternative  to  triosephosphate isomerase for metabolizing
dihydroxyacetone phosphate.

MGS is a small protein of about 13 to 17 kD.  An aspartate residue is involved
in the  catalytic  mechanism.  We  developed a signature pattern that includes
that residue.

-Consensus pattern: [SP]-G-P-[LIVMWY]-G(2)-D-x(0,1)-Q
                    [D 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: April 2006 / Pattern revised.

[ 1] Saadat D., Harrison D.H.T.
     "The crystal structure of methylglyoxal synthase from Escherichia
     coli."
     Structure 7:309-317(1999).
     PubMed=10368300

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}