The domain within your query sequence starts at position 1373 and ends at position 1465; the E-value for the MGS domain shown below is 1.53e-15.

RFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSI
DLVINLPNNNTKFVHDNYVIRRTAVDSGIALLT

MGS

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 4.2.3.3), 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) ].

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

Cellular role (predicted cellular role)

Cellular role: interaction

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
24.08	map00230	Purine metabolism
22.47	map00240	Pyrimidine metabolism
22.24	map00670	One carbon pool by folate
22.13	map00251	Glutamate metabolism
7.07	map00620	Pyruvate metabolism
0.75	map00252	Alanine and aspartate metabolism
0.40	map00910	Nitrogen metabolism
0.40	map00330	Arginine and proline metabolism
0.40	map00220	Urea cycle and metabolism of amino groups
0.06	map00061	Fatty acid biosynthesis

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with MGS domain which could be assigned to a KEGG orthologous group, and not all proteins containing MGS domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of MGS domains in PDB

PDB code	Title
1a9x	CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS
1b93	METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI
1bxr	STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP
1c30	CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S
1c3o	CRYSTAL STRUCTURE OF THE CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTANT C269S WITH BOUND GLUTAMINE
1ce8	CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP
1cs0	Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde
1egh	STRUCTURE OF METHYLGLYOXAL SYNTHASE COMPLEXED WITH THE COMPETITIVE INHIBITOR 2-PHOSPHOGLYCOLATE
1g8m	CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION
1ik4	X-ray Structure of Methylglyoxal Synthase from E. coli Complexed with Phosphoglycolohydroxamic Acid
1jdb	CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI
1kee	Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin
1m6v	Crystal Structure of the G359F (small subunit) Point Mutant of Carbamoyl Phosphate Synthetase
1m9n	CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH AICAR AND XMP AT 1.93 ANGSTROMS.
1oz0	CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH A MULTISUBSTRATE ADDUCT INHIBITOR BETA-DADF.
1p4r	Crystal Structure of Human ATIC in complex with folate-based inhibitor BW1540U88UD
1pkx	Crystal Structure of human ATIC in complex with XMP
1pl0	Crystal structure of human ATIC in complex with folate-based inhibitor, BW2315U89UC
1s89	H98N Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid
1s8a	H98Q Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid
1t36	Crystal structure of E. coli carbamoyl phosphate synthetase small subunit mutant C248D complexed with uridine 5'-monophosphate
1thz	Crystal Structure of Avian AICAR Transformylase in Complex with a Novel Inhibitor Identified by Virtual Ligand Screening
1vmd	Crystal structure of Methylglyoxal synthase (TM1185) from Thermotoga maritima at 2.06 A resolution
1wo8	Crystal structure of methylglyoxal synthase from Thermus thermophilus HB8
1zcz	Crystal structure of Phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase (TM1249) from THERMOTOGA MARITIMA at 1.88 A resolution
2b1g	Crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase
2b1i	crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase
2iu0	crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase
2iu3	crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase
2x8w	The Crystal Structure of Methylglyoxal Synthase from Thermus sp. GH5 Bound to Malonate.
2xw6	The Crystal Structure of Methylglyoxal Synthase from Thermus sp. GH5 Bound to Phosphate Ion.
2yvq	Crystal structure of MGS domain of carbamoyl-phosphate synthetase from homo sapiens
3zzm	Crystal structure of Mycobacterium tuberculosis PurH with a novel bound nucleotide CFAIR, at 2.2 A resolution.
4a1o	Crystal structure of Mycobacterium tuberculosis PurH complexed with AICAR and a novel nucleotide CFAIR, at 2.48 A resolution.
4ehi	An X-ray Crystal Structure of a putative Bifunctional Phosphoribosylaminoimidazolecarboxamide Formyltransferase/IMP Cyclohydrolase
5dot	5DOT
5dou	5DOU
5h3l	5H3L

Links (links to other resources describing this domain)

• PFAM: MGS
• INTERPRO: IPR011607