Q9LDQ7 · METK_CAMSI

  • Protein
    S-adenosylmethionine synthase
  • Gene
    SAM
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Note: Binds 2 divalent ions per subunit. The metal ions interact primarily with the substrate (By similarity).
Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).
K+ (UniProtKB | Rhea| CHEBI:29103 )

Note: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate (By similarity).

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 site9Mg2+ (UniProtKB | ChEBI)
Binding site15ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
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 site167-169ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site235-238ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site246ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site246L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site252-253ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site269ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site273ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site277ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site277L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain

GO annotations

AspectTerm
Cellular Componentcytosol
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
  • Short names
    AdoMet synthase
  • Alternative names
    • Methionine adenosyltransferase (MAT)

Gene names

    • Name
      SAM

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Theaceae > Camellia

Accessions

  • Primary accession
    Q9LDQ7

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003630161-393S-adenosylmethionine synthase

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Sequence similarities

Belongs to the AdoMet synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    393
  • Mass (Da)
    42,800
  • Last updated
    2000-10-01 v1
  • Checksum
    67F3D2C50DA42682
METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDQDSKVACETCTKTNMVMVFGEITTKAAVDYEKIVRDTCRTIGFVSDDVGLDADNCKVLVNIEQQSPDIAQGVHGHLTKRPEEIGAGDQGHMFGYATDETSELMPLSHVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYYNEKGATVPIRVHTLLISTQHDETVTNDEIAADLKEHVIKPVIPDKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVANGLARRCIVQVSYAIGVPEPLSVFVDTYGTGKIPDKEILKIVKESFDFRPGMIAINLDLKRGGNSRFLKTAAYGHFGRDDPDFTWESGEAPQVGQTSS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ277206
EMBL· GenBank· DDBJ
CAB83039.1
EMBL· GenBank· DDBJ
Genomic DNA
AB041534
EMBL· GenBank· DDBJ
BAA94605.1
EMBL· GenBank· DDBJ
mRNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp