A0A202DS98 · A0A202DS98_UNCXX

  • Protein
    S-adenosylmethionine synthase
  • Gene
    metK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • 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 site226-227ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site235ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site235L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site241-242ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site262ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Binding site266L-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
      BVY01_04355

Organism names

Accessions

  • Primary accession
    A0A202DS98

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer; dimer of dimers.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain4-101S-adenosylmethionine synthetase N-terminal
Region99-109Flexible loop
Domain110-227S-adenosylmethionine synthetase central
Domain230-367S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    378
  • Mass (Da)
    41,327
  • Last updated
    2017-10-25 v1
  • MD5 Checksum
    16C4A17B2B8116FA0975B1AF9FB006B1
MSQHYFSSECVTEGHPDKIADQLSDAVLDAVFEDDPHGRVACECYLTTGMVLVGGEITTKTYVDIPRLVRGVIKEIGYTDASLGLDYESCAILNVIQEQSPDIALGVDREGAGDQGIMFGFATRETKELMPLPIMLAHKLTMQLTKVRKDGTLPWLRPDGKSQVTVKYVDGKPEQISAVVIAAQHSPDIDIESIRKEVIAKVITPVLPEDMFDPDDVKYYINPSGRFVRGGPHGDTGLTGRKIIVDTYGGYGSHGGGCFSGKDPTKVDRSASYVARWVAKNLVASGLADVIEVQLAYALGAVEPVSVLVNSFGTGKVSDEKLSEKVRKVFDLTPAGMIRDLDLRRPIYRKTAAYGHFGRELPEFTWESTDRADELLKA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MSYH01000180
EMBL· GenBank· DDBJ
OVE78809.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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