A0A2H6J811 · A0A2H6J811_UNCXX

  • Protein
    S-adenosylmethionine synthase
  • Gene
    metK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site15ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site17Mg2+ (UniProtKB | ChEBI)
Binding site43K+ (UniProtKB | ChEBI)
Binding site56L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site99L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site164-166ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site230-231ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site239ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site239L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site245-246ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site262ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site266ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site270L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain

GO annotations

AspectTerm
Cellular Componentcytosol
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
      BMS3Bbin12_00038

Organism names

Accessions

  • Primary accession
    A0A2H6J811

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer; dimer of dimers.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain3-101S-adenosylmethionine synthetase N-terminal
Region99-109Flexible loop
Domain115-231S-adenosylmethionine synthetase central
Domain233-371S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    389
  • Mass (Da)
    41,808
  • Last updated
    2018-02-28 v1
  • Checksum
    73A4612BFC748745
MNNYLFTSESVSEGHPDKMADQLSDTILDAILAQDPHAHVACETLIKTGMVLFAGEVTTTAAFDAEALARETIARIGYTSSEMGFDAATCAVLSGIGKQSPDIAQGVDRGTAEAQGAGDQGMMFGYATSETDVLMPAPITYAHRLVRRQAEVRKSGVLPWLRPDAKSQVTIRYEKDRPVGIDTVVLSTQHAPDIGERALHEAVMEEIIRPVLPPEWLRRETKVHINPTGRFVVGGPLGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYACRYVAKNIVAAGLAERCEIQLSYAIGVAEPTSISVQTFGTGKVDDDRLVRLVREHFDLRPGGLIRMLDLLRPVYAATAAYGHFGREDAGFPWEATDRAGLLRDAAAVKAVG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BDTV01000005
EMBL· GenBank· DDBJ
GBE46885.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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