CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
Domain Context
CATH Clusters
| Superfamily | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
| Functional Family | 5-aminolevulinate synthase, mitochondrial |
Enzyme Information
| 2.3.1.29 |
Glycine C-acetyltransferase.
based on mapping to UniProt P0AB77
Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate.
-!- Acts in concert with EC 1.1.1.103 in the degradation of threonine to form glycine. -!- This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex.
|
UniProtKB Entries (1)
| P0AB77 |
KBL_ECOLI
Escherichia coli K-12
2-amino-3-ketobutyrate coenzyme A ligase
|
PDB Structure
| PDB | 1FC4 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
Biochemistry
|