MGS-like domain
SMART accession number:SM00851
Description: This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site (PUBMED:10526357).
Interpro abstract (IPR011607):

Methylglyoxal synthase (MGS, EC, which catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to methylglyoxal (MG) and inorganic phosphate, has been found in many organisms, including enteric bacteria, some gram-positive bacteria, a number of archaebacteria, several yeast species and goat liver [ (PUBMED:23592737) (PUBMED:10388730) ].

The main core of the MGS-like domain, a modified 'Rossmann' fold, is characterised by a five stranded parallel beta-sheet flanked on either side by three and five alpha-helices, respectively [ (PUBMED:14756553) (PUBMED:10089390) ]. MGS-like domains share a conserved phosphate binding site [ (PUBMED:10526357) (PUBMED:29063699) ].

Family alignment:
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There are 47239 MGS domains in 47236 proteins in SMART's nrdb database.

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