Q729A3 · METK_NITV2
- ProteinS-adenosylmethionine synthase
- GenemetK
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids391 (go to sequence)
- Protein existenceEvidence at protein level
- 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
- ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
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 | 19 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: H | ||||||
Binding site | 21 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 47 | K+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 60 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: E | ||||||
Binding site | 103 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: Q | ||||||
Binding site | 168-170 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: DGK | ||||||
Binding site | 236-237 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: RF | ||||||
Binding site | 245 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: D | ||||||
Binding site | 245 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: D | ||||||
Binding site | 251-252 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: RK | ||||||
Binding site | 268 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: A | ||||||
Binding site | 272 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: K | ||||||
Binding site | 276 | 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 > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Nitratidesulfovibrio
Accessions
- Primary accessionQ729A3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000174517 | 1-391 | S-adenosylmethionine synthase | |||
Sequence: MIPSKGKYYFTSESVTEGHPDKVADQISDAVLDVLLAQDPNSRVACETLVTTGMAVIAGEITTRGYADLPHVVRETIRNIGYNSSEMGFDWQTCAVISSIDKQSADIAQGVDRATNEDQGAGDQGMMFGFACDETATLMPAPIYWAHQLSQRLTEVRKDGTVDIFRPDGKTQVSFEYVDGKPVRINNVVVSTQHKDSASQADIIDAVKTHVIRPILEPSGFFDEKACDIFINTTGRFVIGGPMGDCGLTGRKIIQDTYGGMGHHGGGAFSGKDASKVDRSGAYMARYIAKNVVASGLAPKCEVQIAYCIGVAEPVSVLVSSQGTASVPDEVLTRAVREVFDLRPFHITRRLDLLRPIYGKTSCYGHFGRELPEFTWEHTDAAADLRTAAKV |
Proteomic databases
Interaction
Subunit
Homotetramer; dimer of dimers.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q729A3 | DVU_0493 Q72ES6 | 2 | EBI-10071362, EBI-10071066 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 103-113 | Flexible loop | ||||
Sequence: QSADIAQGVDR |
Sequence similarities
Belongs to the AdoMet synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length391
- Mass (Da)42,424
- Last updated2004-07-05 v1
- Checksum89E6CF9683547FFD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE017285 EMBL· GenBank· DDBJ | AAS96921.1 EMBL· GenBank· DDBJ | Genomic DNA |