P23686 · METK1_ARATH
- ProteinS-adenosylmethionine synthase 1
- GeneSAM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids393 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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:
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 (By similarity).
Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).
Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).
Note: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate (By similarity).
Activity regulation
Reversibly inhibited by NO. Inhibited by 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) and N-ethylmaleimide (NEM) (in vitro).
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 | 9 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 15 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: H | ||||||
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 | 167-169 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: DGK | ||||||
Binding site | 235-238 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: SGRF | ||||||
Binding site | 246 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: D | ||||||
Binding site | 246 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: D | ||||||
Binding site | 252-253 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: RK | ||||||
Binding site | 269 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: A | ||||||
Binding site | 273 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: K | ||||||
Binding site | 277 | ATP (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: K | ||||||
Binding site | 277 | L-methionine (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | plant-type cell wall | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | methionine adenosyltransferase activity | |
Biological Process | ethylene biosynthetic process | |
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 1
- EC number
- Short namesAdoMet synthase 1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP23686
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 114 | Loss of the NO-mediated inhibition by S-nitrosylation. | ||||
Sequence: C → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000174456 | 1-393 | S-adenosylmethionine synthase 1 | |||
Sequence: METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKATVDYEKIVRDTCRAIGFVSDDVGLDADKCKVLVNIEQQSPDIAQGVHGHFTKCPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCAWLRPDGKTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDEIARDLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQVSYAIGVPEPLSVFVDTYETGLIPDKEILKIVKESFDFRPGMMTINLDLKRGGNGRFLKTAAYGHFGRDDPDFTWEVVKPLKWDKPQA | ||||||
Modified residue | 114 | S-nitrosocysteine | ||||
Sequence: C |
Post-translational modification
S-nitrosylated in the presence of NO. The inhibition of SAM1 activity by S-nitrosylation could contribute to the cross-talk between ethylene and NO signaling.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)43,158
- Last updated2002-06-20 v2
- Checksum27B0AF8AF55D2FF3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4HXK3 | F4HXK3_ARATH | At1g02590 | 89 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 117 | in Ref. 1; AAA32868 | ||||
Sequence: E → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M55077 EMBL· GenBank· DDBJ | AAA32868.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC022521 EMBL· GenBank· DDBJ | AAG10639.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE27437.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE27438.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF325061 EMBL· GenBank· DDBJ | AAG40413.1 EMBL· GenBank· DDBJ | mRNA | ||
AY092955 EMBL· GenBank· DDBJ | AAM12954.1 EMBL· GenBank· DDBJ | mRNA | ||
AF428440 EMBL· GenBank· DDBJ | AAL16209.1 EMBL· GenBank· DDBJ | mRNA | ||
AY052311 EMBL· GenBank· DDBJ | AAK96504.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AY061895 EMBL· GenBank· DDBJ | AAL31222.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AY087703 EMBL· GenBank· DDBJ | AAM65240.1 EMBL· GenBank· DDBJ | mRNA | ||
Z17672 EMBL· GenBank· DDBJ | CAA79031.1 EMBL· GenBank· DDBJ | mRNA | ||
Z17762 EMBL· GenBank· DDBJ | CAA79057.1 EMBL· GenBank· DDBJ | mRNA |