A0A9E5CU88 · A0A9E5CU88_UNCCH
- ProteinS-adenosylmethionine decarboxylase proenzyme
- GenespeD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids143 (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 | 82-83 | Cleavage (non-hydrolytic); by autolysis | ||||
Sequence: ES | ||||||
Active site | 83 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
Sequence: S | ||||||
Active site | 88 | Proton acceptor; for processing activity | ||||
Sequence: H | ||||||
Active site | 103 | Proton donor; for catalytic activity | ||||
Sequence: C |
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
- Strains
- Taxonomic lineageBacteria > Chloroflexota
Accessions
- Primary accessionA0A9E5CU88
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5039765735 | 1-82 | S-adenosylmethionine decarboxylase beta chain | |||
Sequence: MGARVATLDTASEGWCLNARFTSLGIHLLLELKDCNPVILDDIDLIKQVMIGAANEAGATIVGETFHKFSPVGVTGVVAIAE | ||||||
Modified residue | 83 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_5039765736 | 83-143 | S-adenosylmethionine decarboxylase alpha chain | |||
Sequence: SHLCIHTWPEYRYAAADIFTCGEGFKPYEAAKLIVDRLQCKDPSISEVQRGVISQATSTPV |
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
Sequence
- Sequence statusComplete
- Length143
- Mass (Da)15,391
- Last updated2023-05-03 v1
- Checksum1FD91D5E2C4A3A0A