L9KSZ4 · L9KSZ4_TUPCH

Function

function

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
K+ (UniProtKB | Rhea| CHEBI:29103 )

Note: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmethionine adenosyltransferase complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionmethionine adenosyltransferase activity
Biological Processone-carbon metabolic process
Biological ProcessS-adenosylmethionine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    S-adenosylmethionine synthase
  • EC number

Gene names

    • ORF names
      TREES_T100005353

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Scandentia > Tupaiidae > Tupaia

Accessions

  • Primary accession
    L9KSZ4

Proteomes

Interaction

Subunit

Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain. Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-85S-adenosylmethionine synthetase N-terminal
Domain100-220S-adenosylmethionine synthetase central
Domain222-332S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    333
  • Mass (Da)
    36,478
  • Last updated
    2013-04-03 v1
  • Checksum
    56B01CF029B1C59D
DKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAIKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVSS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KB320680
EMBL· GenBank· DDBJ
ELW65609.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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