Q6PTS4 · Q6PTS4_ANTME
- ProteinS-adenosylmethionine synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids321 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
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 | |
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
Organism names
- Taxonomic lineageEukaryota > Metazoa > Echinodermata > Pelmatozoa > Crinoidea > Articulata > Comatulida > Antedonidae > Antedon
Accessions
- Primary accessionQ6PTS4
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-82 | S-adenosylmethionine synthetase N-terminal | ||||
Sequence: ICDQVSDAVLDAHLKQDPYAKVACESVSKTGMILVAGEITSNAHVDYQSVIRNTIKRIGYDDSSKGFDFETRNVLVALEEQA | ||||||
Domain | 98-220 | S-adenosylmethionine synthetase central | ||||
Sequence: IGAGDQGLMFGYATNETEELMPLTVVLAHGLTKKLAEERRKKNGQMSYLRPDCKSQVTVQYRMDDGCCVPLRVHTVVISTQHSGDVTQKQLRKDLADIVIPAVIPAKYLDKDTVFHFNPSGSF | ||||||
Domain | 222-320 | S-adenosylmethionine synthetase C-terminal | ||||
Sequence: IGGPKGGAGLTGRKIIVDTYGGWGAHGGGAFSGKDMTKVDRSAAYAARWVAKSLVAANVCKRALVQVAYAIGIAEPLSVTVWDYGTSDKSQDELLKLVN |
Sequence similarities
Belongs to the AdoMet synthase family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length321
- Mass (Da)34,766
- Last updated2004-07-05 v1
- Checksum831023A14DEF19CB
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: I | ||||||
Non-terminal residue | 321 | |||||
Sequence: D |