A0A6B9FK27 · A0A6B9FK27_9HYPH

Function

function

Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.

Catalytic activity

Cofactor

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

Note: Binds 1 potassium ion per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 divalent ions per subunit.

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site17ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site19Mg2+ (UniProtKB | ChEBI)
Binding site45K+ (UniProtKB | ChEBI)
Binding site58L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site102L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site169-171ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site235-236ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site244ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site244L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site250-251ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site267ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site271ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site275L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium 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
  • Short names
    AdoMet synthase
  • Alternative names
    • MAT
    • Methionine adenosyltransferase

Gene names

    • Name
      metK
    • ORF names
      MMSR116_09490

Organism names

Accessions

  • Primary accession
    A0A6B9FK27

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer; dimer of dimers.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain5-104S-adenosylmethionine synthetase N-terminal
Region102-112Flexible loop
Domain118-236S-adenosylmethionine synthetase central
Domain238-380S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    392
  • Mass (Da)
    41,896
  • Last updated
    2020-06-17 v1
  • Checksum
    528E12AD965DA67D
MPRSNYLFTSESVSEGHPDKVCDRISDTVVDAYLTAMPEARLGVETLATTNRIVIAGEVRGPDSVTFKDLEALTREAVKDIGYEQSGFHWKNNDVAIHLHAQSADIAQGVDAAGNKDEGAGDQGIMFGYAADETPELMPAPIFYAHRILKDLADARRAKQGDAAKLGPDAKSQVTVRYENGRPVEVTQIVLSTQHLDESLDSADVRAIVEPYIRKALPEGWVNEGTVWHVNPTGKFVIGGPDGDAGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYAARYLAKNVVAAGLARRATIQLAYAIGVSKPLSIYVDLHGTGNVDEAKLEAVLMDALDLSPRGIRTALGLNKPIYARTSAYGHFGRAPEADGGFSWERTDLADKLKSALA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP043538
EMBL· GenBank· DDBJ
QGY02086.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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