B8LFH4 · B8LFH4_IPOBA
- ProteinS-adenosylmethionine synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids393 (go to sequence)
- Protein existenceEvidence at transcript level
- 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
- ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
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. Can utilize magnesium, manganese or cobalt (in vitro).
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 > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Solanales > Convolvulaceae > Ipomoeeae > Ipomoea
Accessions
- Primary accessionB8LFH4
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-101 | S-adenosylmethionine synthetase N-terminal | ||||
Sequence: FLFTSESVNEGHPDKLCDQVSDAVLDACLAQDPESKVACETCTKTNMVMVFGEITTKAEIDYEKIVRDTCRAIGFVSDDVGLDADNCKVLVNIEQQSP | ||||||
Domain | 118-238 | S-adenosylmethionine synthetase central | ||||
Sequence: IGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKDGTCAWLRPDGKTQVTVEYYNDNGAMVPVRVHTVLISTQHDETVTNDEIARDLKEHVIKPVIPEKYLDEKTIFHLNPSGRF | ||||||
Domain | 240-381 | S-adenosylmethionine synthetase C-terminal | ||||
Sequence: IGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYVVRQAAKSIVANGLARRCIVQVSYAIGVPEPLSVFVDTYGTGKIPDKEILKIVKEHFDFRPGMIAINLDLKRGGNSRFLKTAAYGHFGRDDPDFTWE |
Sequence similarities
Belongs to the AdoMet synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)43,095
- Last updated2009-03-03 v1
- Checksum7BD0D6DED6C1A1C0