A0A1Q4F4I1 · A0A1Q4F4I1_9SPHI

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 site14ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site16Mg2+ (UniProtKB | ChEBI)
Binding site42K+ (UniProtKB | ChEBI)
Binding site55L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site98L-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 site240-241ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site249ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site249L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site255-256ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site272ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site276ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site280L-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
      BGP14_20655

Organism names

Accessions

  • Primary accession
    A0A1Q4F4I1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer; dimer of dimers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain3-100S-adenosylmethionine synthetase N-terminal
Region98-108Flexible loop
Domain113-241S-adenosylmethionine synthetase central
Domain243-378S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    417
  • Mass (Da)
    46,043
  • Last updated
    2017-04-12 v1
  • Checksum
    2C4D25BC743CAA80
MPYLFTSESVSEGHPDKVADQISDAIIDNFLAFDPNSKVACETLVTTGQVVLAGEVKSRAYLDVQEIARGVIRKIGYTKSEYMFEAHSCGVLSAIHEQSADINQGVDRKKKEDQGAGDQGMMFGYATDETDDYMPLSLDLAHKILIELSALRREGKQIKYLRPDAKSQVTLEYDDNNRPVRIDAIVVSTQHDDFDTEARMLEKIKNDIINILIPRVKAKYKKYAKLFNKDIKYHINPTGKFVIGGPHGDTGLTGRKIIVDTYGGKGAHGGGAFSGKDPSKVDRSAAYATRHIAKNLVAAGVAGEVLVQVSYAIGVAKPTSINVNTFGTARVDLTDGEIGKIVEGLFDMRPYFIEKRLKLRTPIYSETAAYGHMGRKPVKVTKTFTSPDGKTKKVNVELFTWEKLDKVKEVKKAFGLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MKWG01000027
EMBL· GenBank· DDBJ
OJY86385.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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