P17562 · METK2_ARATH
- ProteinS-adenosylmethionine synthase 2
- GeneSAM2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids393 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Cofactor
Protein has several cofactor binding sites:
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).
Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 15 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: H | ||||||
Binding site | 43 | K+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 56 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: E | ||||||
Binding site | 99 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: Q | ||||||
Binding site | 167-169 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: DGK | ||||||
Binding site | 235-238 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: SGRF | ||||||
Binding site | 246 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: D | ||||||
Binding site | 246 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: D | ||||||
Binding site | 252-253 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: RK | ||||||
Binding site | 269 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: A | ||||||
Binding site | 273 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: K | ||||||
Binding site | 277 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: K | ||||||
Binding site | 277 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | nucleolus | |
Cellular Component | plant-type cell wall | |
Cellular Component | plasmodesma | |
Molecular Function | ATP binding | |
Molecular Function | copper ion binding | |
Molecular Function | methionine adenosyltransferase activity | |
Biological Process | one-carbon metabolic process | |
Biological Process | S-adenosylmethionine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameS-adenosylmethionine synthase 2
- EC number
- Short namesAdoMet synthase 2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP17562
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000174457 | 1-393 | S-adenosylmethionine synthase 2 | |||
Sequence: METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKATIDYEKIVRDTCRSIGFISDDVGLDADKCKVLVNIEQQSPDIAQGVHGHFTKRPEDIGAGDQGHMFGYATDETPELMPLSHVLATKIGARLTEVRKNGTCRWLRPDGKTQVTVEYYNDNGAMVPVRVHTVLISTQHDETVTNDEIARDLKEHVIKPIIPEKYLDDKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQVSYAIGVPEPLSVFVDTYGTGLIPDKEILKIVKETFDFRPGMMTINLDLKRGGNGRFQKTAAYGHFGRDDPDFTWEVVKPLKWDKPQA |
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)43,255
- Last updated1990-08-01 v1
- ChecksumCE008EA565FD1FBC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |