Function and Biology Details
Reaction catalysed:
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Succinyl-CoA synthetase-like
- CoA-binding
- ATP-citrate lyase/succinyl-CoA ligase, active site
- ATP-citrate lyase/succinyl-CoA ligase, conserved site
- ATP-citrate synthase/succinyl-CoA ligase, C-terminal domain
- NAD(P)-binding domain superfamily
- Citrate synthase
- Succinyl-CoA synthetase, beta subunit, conserved site
2 more domains
Structure analysis Details
Assemblies composition:
Assembly name:
ATP-citrate synthase (preferred)
PDBe Complex ID:
PDB-CPX-156798 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-citrate synthase
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 47.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: ATP citrate lyase citrate-binding
Structure domains:
Length: 425 amino acids
Theoretical weight: 47.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P53396 (Residues: 1-425; Coverage: 39%)
Sequence domains: ATP citrate lyase citrate-binding
Structure domains:
ATP-citrate synthase
Molecule details ›
Chain: B
Length: 334 amino acids
Theoretical weight: 36.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 334 amino acids
Theoretical weight: 36.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P53396 (Residues: 487-820; Coverage: 30%)
Sequence domains:
Structure domains:
