Function and Biology Details
Reaction catalysed:
A 2-oxo acid = an aldehyde + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Thiamin diphosphate-binding fold
- Pyruvate decarboxylase/indolepyruvate decarboxylase-like
- TPP-binding enzyme, conserved site
- Thiamine pyrophosphate enzyme, TPP-binding
- Pyruvate decarboxylase/indolepyruvate decarboxylase-like, PP-binding domain
- Thiamine pyrophosphate enzyme, central domain
- DHS-like NAD/FAD-binding domain superfamily
- Pyruvate decarboxylase/indolepyruvate decarboxylase-like, pyrimidine-binding domain
1 more domain
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Pyruvate decarboxylase (preferred)
PDBe Complex ID:
PDB-CPX-139129 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate decarboxylase
Molecule details ›
Chains: A, B, E, F, V, X, Y, Z
Length: 568 amino acids
Theoretical weight: 60.99 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli DH5[alpha]
UniProt:
Sequence domains:
Length: 568 amino acids
Theoretical weight: 60.99 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli DH5[alpha]
UniProt:
- Canonical:
P06672 (Residues: 1-568; Coverage: 100%)
Sequence domains:
- Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
- Thiamine pyrophosphate enzyme, central domain
- Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID23-1
Spacegroup:
P1
Expression system: Escherichia coli DH5[alpha]
