CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| Functional Family | 2-amino-3-ketobutyrate coenzyme A ligase |
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
|
