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-185217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
pyruvate decarboxylase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 573 amino acids
Theoretical weight: 61.88 KDa
Source organism: Zymobacter palmae
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Length: 573 amino acids
Theoretical weight: 61.88 KDa
Source organism: Zymobacter palmae
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q8KTX6 (Residues: 1-556; Coverage: 100%)
Sequence domains:
