Function and Biology Details
Reaction catalysed:
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Pyruvate, phosphate dikinase
- Pyruvate kinase-like domain superfamily
- PEP-utilising enzyme, C-terminal
- Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
- PEP-utilising enzyme, active site
- PEP-utilising enzyme, mobile domain
- Phosphohistidine domain superfamily
- Pyruvate phosphate dikinase, AMP/ATP-binding
1 more domain
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Pyruvate, phosphate dikinase (preferred)
PDBe Complex ID:
PDB-CPX-131223 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate, phosphate dikinase
Molecule details ›
Chain: A
Length: 913 amino acids
Theoretical weight: 100.54 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Length: 913 amino acids
Theoretical weight: 100.54 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
O76283 (Residues: 1-913; Coverage: 100%)
Sequence domains:
- Pyruvate phosphate dikinase, AMP/ATP-binding domain
- PEP-utilising enzyme, mobile domain
- PEP-utilising enzyme, PEP-binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
LURE BEAMLINE DW32
Spacegroup:
P21212
Expression system: Escherichia coli BL21
