A0A2H6J811 · A0A2H6J811_UNCXX
- ProteinS-adenosylmethionine synthase
- GenemetK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids389 (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 1 potassium ion per subunit.
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.
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
- Organism
- Taxonomic lineageBacteria
Accessions
- Primary accessionA0A2H6J811
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer; dimer of dimers.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-101 | S-adenosylmethionine synthetase N-terminal | ||||
Sequence: NYLFTSESVSEGHPDKMADQLSDTILDAILAQDPHAHVACETLIKTGMVLFAGEVTTTAAFDAEALARETIARIGYTSSEMGFDAATCAVLSGIGKQSP | ||||||
Region | 99-109 | Flexible loop | ||||
Sequence: QSPDIAQGVDR | ||||||
Domain | 115-231 | S-adenosylmethionine synthetase central | ||||
Sequence: QGAGDQGMMFGYATSETDVLMPAPITYAHRLVRRQAEVRKSGVLPWLRPDAKSQVTIRYEKDRPVGIDTVVLSTQHAPDIGERALHEAVMEEIIRPVLPPEWLRRETKVHINPTGRF | ||||||
Domain | 233-371 | S-adenosylmethionine synthetase C-terminal | ||||
Sequence: VGGPLGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYACRYVAKNIVAAGLAERCEIQLSYAIGVAEPTSISVQTFGTGKVDDDRLVRLVREHFDLRPGGLIRMLDLLRPVYAATAAYGHFGREDAGFPWE |
Sequence similarities
Belongs to the AdoMet synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length389
- Mass (Da)41,808
- Last updated2018-02-28 v1
- Checksum73A4612BFC748745