L9KSZ4 · L9KSZ4_TUPCH
- ProteinS-adenosylmethionine synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids333 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- L-methionine + ATP + H2O = S-adenosyl-L-methionine + phosphate + diphosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Note: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Pathway
Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | methionine adenosyltransferase complex | |
Molecular Function | ATP binding | |
Molecular Function | metal 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
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Scandentia > Tupaiidae > Tupaia
Accessions
- Primary accessionL9KSZ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain. Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-85 | S-adenosylmethionine synthetase N-terminal | ||||
Sequence: DKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAIKHIGYDDSSKGFDYKTCNVLVALEQQSP | ||||||
Domain | 100-220 | S-adenosylmethionine synthetase central | ||||
Sequence: IGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRF | ||||||
Domain | 222-332 | S-adenosylmethionine synthetase C-terminal | ||||
Sequence: IGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVS |
Sequence similarities
Belongs to the AdoMet synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length333
- Mass (Da)36,478
- Last updated2013-04-03 v1
- Checksum56B01CF029B1C59D
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: D |
Keywords
- Technical term