Function and Biology Details
Reaction catalysed:
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assemblies composition:
Assembly name:
S-adenosylmethionine decarboxylase proenzyme (preferred)
PDBe Complex ID:
PDB-CPX-194591 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
S-adenosylmethionine decarboxylase beta chain
Molecule details ›
Chains: B, D
Length: 62 amino acids
Theoretical weight: 7 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains: S-adenosylmethionine decarboxylase
Structure domains: S-adenosylmethionine decarboxylase domain
Length: 62 amino acids
Theoretical weight: 7 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9WZC3 (Residues: 1-62; Coverage: 48%)
Sequence domains: S-adenosylmethionine decarboxylase
Structure domains: S-adenosylmethionine decarboxylase domain
S-adenosylmethionine decarboxylase alpha chain
Molecule details ›
Chains: A, C
Length: 68 amino acids
Theoretical weight: 7.81 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains: S-adenosylmethionine decarboxylase
Structure domains: Double Stranded RNA Binding Domain
Length: 68 amino acids
Theoretical weight: 7.81 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical: Q9WZC3 (Residues: 64-130; Coverage: 52%)
Sequence domains: S-adenosylmethionine decarboxylase
Structure domains: Double Stranded RNA Binding Domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RU300
Spacegroup:
R3
Expression system: Escherichia coli
