P23686 · METK1_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

Reversibly inhibited by NO. 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 region
Cellular Componentplant-type cell wall
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionmethionine adenosyltransferase activity
Biological Processethylene biosynthetic process
Biological Processone-carbon metabolic process
Biological ProcessS-adenosylmethionine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    S-adenosylmethionine synthase 1
  • EC number
  • Short names
    AdoMet synthase 1
  • Alternative names
    • Methionine adenosyltransferase 1 (MAT 1)

Gene names

    • Name
      SAM1
    • ORF names
      T14P4.17, T14P4_22
    • Ordered locus names
      At1g02500

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
    P23686
  • Secondary accessions
    • Q941A8
    • Q9FEE0

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis114Loss of the NO-mediated inhibition by S-nitrosylation.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001744561-393S-adenosylmethionine synthase 1
Modified residue114S-nitrosocysteine

Post-translational modification

S-nitrosylated in the presence of NO. The inhibition of SAM1 activity by S-nitrosylation could contribute to the cross-talk between ethylene and NO signaling.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in stems and roots.

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)
    43,158
  • Last updated
    2002-06-20 v2
  • Checksum
    27B0AF8AF55D2FF3
METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKATVDYEKIVRDTCRAIGFVSDDVGLDADKCKVLVNIEQQSPDIAQGVHGHFTKCPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCAWLRPDGKTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDEIARDLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQVSYAIGVPEPLSVFVDTYETGLIPDKEILKIVKESFDFRPGMMTINLDLKRGGNGRFLKTAAYGHFGRDDPDFTWEVVKPLKWDKPQA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F4HXK3F4HXK3_ARATHAt1g0259089

Sequence caution

The sequence AAK96504.1 differs from that shown. Reason: Frameshift
The sequence AAL31222.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict117in Ref. 1; AAA32868

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M55077
EMBL· GenBank· DDBJ
AAA32868.1
EMBL· GenBank· DDBJ
Genomic DNA
AC022521
EMBL· GenBank· DDBJ
AAG10639.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE27437.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE27438.1
EMBL· GenBank· DDBJ
Genomic DNA
AF325061
EMBL· GenBank· DDBJ
AAG40413.1
EMBL· GenBank· DDBJ
mRNA
AY092955
EMBL· GenBank· DDBJ
AAM12954.1
EMBL· GenBank· DDBJ
mRNA
AF428440
EMBL· GenBank· DDBJ
AAL16209.1
EMBL· GenBank· DDBJ
mRNA
AY052311
EMBL· GenBank· DDBJ
AAK96504.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AY061895
EMBL· GenBank· DDBJ
AAL31222.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AY087703
EMBL· GenBank· DDBJ
AAM65240.1
EMBL· GenBank· DDBJ
mRNA
Z17672
EMBL· GenBank· DDBJ
CAA79031.1
EMBL· GenBank· DDBJ
mRNA
Z17762
EMBL· GenBank· DDBJ
CAA79057.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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