A0A2N0L2A6 · A0A2N0L2A6_9CHLR

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 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 site101L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site177-179ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site243-244ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site252ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site252L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site258-259ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site275ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site279ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site283L-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
      BZY82_11815

Organism names

Accessions

  • Primary accession
    A0A2N0L2A6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer; dimer of dimers.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain6-102S-adenosylmethionine synthetase N-terminal
Region101-111Flexible loop
Domain128-244S-adenosylmethionine synthetase central
Domain246-385S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    399
  • Mass (Da)
    42,937
  • Last updated
    2018-04-25 v1
  • Checksum
    24A6118666FA1911
MSSPSYLFTSESVTEGHPDKLCDQVSDAVLDALMAKDPECRVACETAVTTGLVVVMGEVTTNTYVDIPEIVRETIRNIGYTDAAYGIDFHTCGVMVSVKEQSQDISSAVGTSLEARDATSVADETEALGAGDQGMMVGFACTETPELMPLPISLSHALCKRLSTVRREGLLSYLRPDGKSQVTIEYARGVPKRIHTVVLSAQHGPEVSLAQLQRDLREHVVNPILPKKLIDDETKYFVNPSGKFELGGPHADTGLTGRKILVDTYGGAARHGGGAFSGKDPTKVDRSGAYAARYVAKNVVAAGLAERVEVQVSYAIGVAKPISISVETFGTGLVSDEVITGLIDKHFDLRPAAIIEDMKLRRPIFSQTASFGHFGREDIDVPWERTDKAVILRSEAGIL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MUCQ01000100
EMBL· GenBank· DDBJ
PKB64220.1
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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