P17562 · METK2_ARATH

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).

Activity regulation

Inhibited by 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) and N-ethylmaleimide (NEM) (in vitro).

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
Cellular Componentextracellular exosome
Cellular Componentnucleolus
Cellular Componentplant-type cell wall
Cellular Componentplasmodesma
Molecular FunctionATP binding
Molecular Functioncopper 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 2
  • EC number
  • Short names
    AdoMet synthase 2
  • Alternative names
    • Methionine adenosyltransferase 2 (MAT 2)

Gene names

    • Name
      SAM2
    • ORF names
      T7B11.11
    • Ordered locus names
      At4g01850

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    P17562
  • Secondary accessions
    • Q42263

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001744571-393S-adenosylmethionine synthase 2

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in stems and roots (PubMed:2482229).
Detected in trichomes (at the protein level) (PubMed:15276459).

Gene expression databases

Interaction

Subunit

Homotetramer (By similarity).
Interacts with GRF3

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the AdoMet synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    393
  • Mass (Da)
    43,255
  • Last updated
    1990-08-01 v1
  • Checksum
    CE008EA565FD1FBC
METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKATIDYEKIVRDTCRSIGFISDDVGLDADKCKVLVNIEQQSPDIAQGVHGHFTKRPEDIGAGDQGHMFGYATDETPELMPLSHVLATKIGARLTEVRKNGTCRWLRPDGKTQVTVEYYNDNGAMVPVRVHTVLISTQHDETVTNDEIARDLKEHVIKPIIPEKYLDDKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQVSYAIGVPEPLSVFVDTYGTGLIPDKEILKIVKETFDFRPGMMTINLDLKRGGNGRFQKTAAYGHFGRDDPDFTWEVVKPLKWDKPQA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M33217
EMBL· GenBank· DDBJ
AAA32869.1
EMBL· GenBank· DDBJ
Genomic DNA
AC007138
EMBL· GenBank· DDBJ
AAD22647.1
EMBL· GenBank· DDBJ
Genomic DNA
AL161493
EMBL· GenBank· DDBJ
CAB80678.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE82084.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE82085.1
EMBL· GenBank· DDBJ
Genomic DNA
AY072327
EMBL· GenBank· DDBJ
AAL61934.1
EMBL· GenBank· DDBJ
mRNA
AY094454
EMBL· GenBank· DDBJ
AAM19825.1
EMBL· GenBank· DDBJ
mRNA
BT000575
EMBL· GenBank· DDBJ
AAN18144.1
EMBL· GenBank· DDBJ
mRNA
Z33778
EMBL· GenBank· DDBJ
CAA83930.1
EMBL· GenBank· DDBJ
mRNA
Z29136
EMBL· GenBank· DDBJ
CAA82393.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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