Q9I5R7 · SPED_PSEAE
- ProteinS-adenosylmethionine decarboxylase proenzyme
- GenespeD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids264 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Catalytic activity
- S-adenosyl-L-methionine + H+ = S-adenosyl 3-(methylsulfanyl)propylamine + CO2
Cofactor
Note: Binds 1 pyruvoyl group covalently per subunit.
Pathway
Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 112-113 | Cleavage (non-hydrolytic); by autolysis | |||
Active site | 113 | Schiff-base intermediate with substrate; via pyruvic acid | |||
Active site | 118 | Proton acceptor; for processing activity | |||
Active site | 141 | Proton donor; for catalytic activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenosylmethionine decarboxylase activity | |
Biological Process | spermidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameS-adenosylmethionine decarboxylase proenzyme
- EC number
- Short namesAdoMetDC ; SAMDC
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9I5R7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000030053 | 1-112 | S-adenosylmethionine decarboxylase beta chain | ||
Modified residue | 113 | Pyruvic acid (Ser); by autocatalysis | |||
Chain | PRO_0000030054 | 113-264 | S-adenosylmethionine decarboxylase alpha chain | ||
Post-translational modification
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length264
- Mass (Da)30,478
- Last updated2001-03-01 v1
- Checksum6181DA3988042C65
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004091 EMBL· GenBank· DDBJ | AAG04043.1 EMBL· GenBank· DDBJ | Genomic DNA |