A0A350M015 · A0A350M015_UNCXX

  • Protein
    S-adenosylmethionine synthase
  • Gene
    metK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • 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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site159-161ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site225-226ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site234ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site234L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site240-241ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site261ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site265L-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
      DCX16_04205

Organism names

Accessions

  • Primary accession
    A0A350M015

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer; dimer of dimers.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain4-100S-adenosylmethionine synthetase N-terminal
Region99-109Flexible loop
Domain111-226S-adenosylmethionine synthetase central
Domain228-367S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    375
  • Mass (Da)
    41,655
  • Last updated
    2018-11-07 v1
  • Checksum
    F0230298B36023A0
MEDFLFTSESVTEGHPDKIADQISDGVLDAIIKEDPNGRVACECLITTGLAFVAGEITTSCYVNITQVVRDIVRDVGYIDPEYGFDYESCAVITAIQEQSSDIAQGVDIGGAGDQGMMFGYATNETPELMPMPILLAHKLTKRLSYVRKHKILDWVRPDGKSQVTVEYIDGKPKRVRTVIIACQHDPEIECSELRDAVMDEVIKKIIPESMLDKETKFFINPTGRFVIGGPQGDTGLTGRKIIVDTYGGWGRHGGGCFSGKDPTKVDRSASYMARYLAKNIVAGEVTESCEVQLAYAIGVSEPIAIMVTTKGKSKKSNEELVEIIKRNFDLSPKGIIDFLDLRRPIFRKTAVYGHFGREEPEFSWEKVDKKELFM

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DNCM01000111
EMBL· GenBank· DDBJ
HAW50132.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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