Function and Biology Details
Reactions catalysed:
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Succinate--CoA ligase-like, beta subunit
- Succinyl-CoA synthetase-like
- Succinyl-CoA ligase, alpha subunit
- ATP-citrate synthase/succinyl-CoA ligase, C-terminal domain
- CoA-binding
- Succinyl-CoA synthetase, beta subunit, conserved site
- ATP-grasp fold, subdomain 1
- ATP-grasp fold, succinyl-CoA synthetase-type
4 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Succinyl-CoA Synthetase (preferred)
PDBe Complex ID:
PDB-CPX-127591 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 32.17 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 305 amino acids
Theoretical weight: 32.17 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O19069 (Residues: 43-346; Coverage: 88%)
Sequence domains:
Structure domains:
Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
Molecule details ›
Chain: B
Length: 395 amino acids
Theoretical weight: 42.64 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 395 amino acids
Theoretical weight: 42.64 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P53590 (Residues: 39-433; Coverage: 91%)
Sequence domains:
Structure domains:
