B5XM14 · METK_STRPZ

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:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 divalent ions per subunit.
K+ (UniProtKB | Rhea| CHEBI:29103 )

Note: Binds 1 potassium ion 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 site16ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site18Mg2+ (UniProtKB | ChEBI)
Binding site44K+ (UniProtKB | ChEBI)
Binding site57L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site100L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site174-176ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site241-242ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site250ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site250L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site256-257ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site273ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site277ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site281L-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
    • Ordered locus names
      Spy49_1083c

Organism names

Accessions

  • Primary accession
    B5XM14

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000930941-398S-adenosylmethionine synthase

Interaction

Subunit

Homotetramer; dimer of dimers.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region100-110Flexible loop

Sequence similarities

Belongs to the AdoMet synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    398
  • Mass (Da)
    43,117
  • Last updated
    2008-11-25 v1
  • Checksum
    B8C95F496B208705
MSERKLFTSESVSEGHPDKIADQISDAILDAILAEDPEAHVAAETCVYTGSVHVFGEISTTAYIDINRVVRDTIAEIGYTEAEYGFSAESVGVHPSLVEQSGDIAQGVNEALESREGDTDDLSHIGAGDQGLMFGFAINETPELMPLPISLSHQLVRRLAELRKSGEISYLRPDAKSQVTVEYDEHDKPVRVDTVVISTQHDPEATNDQIRQDVIEKVIKAVIPADYLDDDTKFFINPTGRFVIGGPQGDSGLTGRKIIVDTYGGYSRHGGGAFSGKDATKVDRSASYAARYIAKNLVAAGLATKAEVQLAYAIGVAQPVSVRVDTFGTSTVPEAVLEAAVRQVFDLRPAGIIQMLDLKRPIYKQTAAYGHMGRTDIDLPWERLNKVDALVEAVKTVL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000829
EMBL· GenBank· DDBJ
ACI61376.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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