Q12QA6 · METK_SHEDO
- ProteinS-adenosylmethionine synthase
- GenemetK
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids383 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- L-methionine + ATP + H2O = S-adenosyl-L-methionine + phosphate + diphosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 divalent ions per subunit.
Note: Binds 1 potassium ion 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 15 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: H | ||||||
Binding site | 17 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
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 | 164-166 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: DAK | ||||||
Binding site | 230-231 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: RF | ||||||
Binding site | 239 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: D | ||||||
Binding site | 239 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: D | ||||||
Binding site | 245-246 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: RK | ||||||
Binding site | 262 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: A | ||||||
Binding site | 266 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: K | ||||||
Binding site | 270 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | magnesium 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
- EC number
- Short namesAdoMet synthase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Alteromonadales > Shewanellaceae > Shewanella
Accessions
- Primary accessionQ12QA6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000302975 | 1-383 | S-adenosylmethionine synthase | |||
Sequence: MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEVTTSAWVDIEEITRKTVREIGYTHSDMGFDADSCAVLNAIGKQSPDINQGVDRADPAEQGAGDQGLMFGYANNETDVLMPAPITYAHALVKRQSEVRKDGTLPWLRPDAKSQVTFAYEDGKIVGIDAIVLSTQHREDVTQADLIEGVMETIIKPVLPAQWLNKDTKYFINPTGRFVIGGPVGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSISIETFGTGKVSEEVLIKLVRQHFELRPYGLTAMLDLARPIYQQTAAYGHFGREGFPWEATDKAEMLRADAGL |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 99-109 | Flexible loop | ||||
Sequence: QSPDINQGVDR |
Sequence similarities
Belongs to the AdoMet synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length383
- Mass (Da)41,455
- Last updated2006-08-22 v1
- Checksum175E654CC92BAEB6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000302 EMBL· GenBank· DDBJ | ABE54370.1 EMBL· GenBank· DDBJ | Genomic DNA |