Function and Biology Details
Reaction catalysed:
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Delta-1-pyrroline-5-carboxylate dehydrogenase
- Aldehyde dehydrogenase, cysteine active site
- Aldehyde dehydrogenase, C-terminal
- Aldehyde dehydrogenase, glutamic acid active site
- Aldehyde dehydrogenase domain
- Aldehyde dehydrogenase, N-terminal
- Aldehyde/histidinol dehydrogenase
- Chaperonin-like RbcX superfamily
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Molecule details ›
Chains: A, B, C, D
Length: 566 amino acids
Theoretical weight: 62.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Aldehyde dehydrogenase family
Structure domains:
Length: 566 amino acids
Theoretical weight: 62.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P30038 (Residues: 18-563; Coverage: 97%)
Sequence domains: Aldehyde dehydrogenase family
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 24-ID-C
Spacegroup:
P65
Expression system: Escherichia coli BL21(DE3)
