G3DSA:3.30.300.280

S-adenosylmethionine synthetase, C-terminal domain

CATH-Gene3D entry
Member databaseCATH-Gene3D
CATH-Gene3D typehomologous superfamily

Description
Imported from IPR042544

S-adenosylmethionine synthetase (MAT,
2.5.1.6
) is the enzyme that catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP
[2]
. AdoMet is an important methyl donor for transmethylation and is also the propylamino donor in polyamine biosynthesis.

In bacteria there is a single isoform of AdoMet synthetase (gene metK), there are two in budding yeast (genes SAM1 and SAM2) and in mammals while in plants there is generally a multigene family.

The sequence of AdoMet synthetase is highly conserved throughout isozymes and species. The active sites of both the Escherichia coli and rat liver MAT reside between two subunits, with contributions from side chains of residues from both subunits, resulting in a dimer as the minimal catalytic entity. The side chains that contribute to the ligand binding sites are conserved between the two proteins. In the structures of complexes with the E. coli enzyme, the phosphate groups have the same positions in the (PPi plus Pi) complex and the (ADP plus Pi) complex and are located at the bottom of a deep cavity with the adenosyl group nearer the entrance
[1]
.

This superfamily represents the C-terminal domain found in S-adenosylmethionine synthase. Structurally, this domain consists of 6 β strands and 3 α helices. Within S-adenosylmethionine synthetase, the domain is not made up a contiguous polypeptide chain, and has some residues contributed from regions away from the C-terminal.

References
Imported from IPR042544

1.[Nature of vitamin K deficiency in the infant age] Sajkovski M, Simonce N, Dejanov I, Janicijevic D, Orglert G, Gligorieva B, Bojadziev L. 21, 299-302, (1975). PMID: 1213535

2.Molecular cloning and nucleotide sequence of cDNA encoding the rat kidney S-adenosylmethionine synthetase. Horikawa S, Sasuga J, Shimizu K, Ozasa H, Tsukada K. J. Biol. Chem. 265, 13683-6, (1990). View articlePMID: 1696256

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.