Q27883 · DCAM_ONCVO
- ProteinS-adenosylmethionine decarboxylase proenzyme
- Genesmd-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
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 active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 31 | ||||
Active site | 34 | ||||
Site | 86-87 | Cleavage (non-hydrolytic); by autolysis | |||
Active site | 87 | Schiff-base intermediate with substrate; via pyruvic acid | |||
Active site | 101 | Proton donor; for catalytic activity | |||
Active site | 248 | Proton acceptor; for processing activity | |||
Active site | 263 | Proton acceptor; for processing activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenosylmethionine decarboxylase activity | |
Biological Process | spermidine biosynthetic process | |
Biological Process | spermine 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
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Spiruromorpha > Filarioidea > Onchocercidae > Onchocerca
Accessions
- Primary accessionQ27883
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000029977 | 1-86 | S-adenosylmethionine decarboxylase beta chain | ||
Modified residue | 87 | Pyruvic acid (Ser); by autocatalysis | |||
Chain | PRO_0000029978 | 87-365 | 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 (By similarity).
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length365
- Mass (Da)41,893
- Last updated1996-11-01 v1
- ChecksumF8615CE029BA40B8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X95714 EMBL· GenBank· DDBJ | CAA65018.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X95713 EMBL· GenBank· DDBJ | CAA65017.1 EMBL· GenBank· DDBJ | mRNA |