A0A0X8IAU9 · A0A0X8IAU9_9CREN
- ProteinS-adenosylmethionine decarboxylase proenzyme
- GenespeH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids125 (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 | 72-73 | Cleavage (non-hydrolytic); by autolysis | |||
Active site | 73 | Schiff-base intermediate with substrate; via pyruvic acid | |||
Active site | 78 | Proton acceptor; for processing activity | |||
Active site | 93 | 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
- Organism
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Acidilobales > Acidilobaceae > Acidilobus
Accessions
- Primary accessionA0A0X8IAU9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5023454478 | 1-72 | S-adenosylmethionine decarboxylase beta chain | ||
Modified residue | 73 | Pyruvic acid (Ser); by autocatalysis | |||
Chain | PRO_5023454479 | 73-125 | 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
Interaction
Subunit
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Structure
Family & Domains
Sequence similarities
Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length125
- Mass (Da)13,959
- Last updated2016-04-13 v1
- MD5 ChecksumB64E49ECD9D1CFA71D14054492ACBA38
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP010515 EMBL· GenBank· DDBJ | AMD31358.1 EMBL· GenBank· DDBJ | Genomic DNA |