CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.12780 | N-terminal domain of ligase-like |
Domain Context
CATH Clusters
| Superfamily | N-terminal domain of ligase-like |
| Functional Family | D-alanine--D-alanyl carrier protein ligase |
Enzyme Information
| 6.2.1.54 |
D-alanine--[D-alanyl-carrier protein] ligase.
based on mapping to UniProt Q81G39
ATP + D-alanine + holo-[D-alaninyl-carrier protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier protein].
-!- The enzyme is involved in the modification of wall teichoic acids, as well as type I and IV lipoteichoic acids, with D-alanine residues. -!- It activates D-alanine using ATP to form a high-energy (D-alanyl)adenylate intermediate and subsequently transfers the alanyl moiety to the phosphopantheinyl prosthetic group of a D-alanyl-carrier protein (DltC).
|
UniProtKB Entries (1)
| Q81G39 |
DLTA_BACCR
Bacillus cereus ATCC 14579
D-alanine--D-alanyl carrier protein ligase
|
PDB Structure
| PDB | 3DHV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure and enantiomer selection by D-alanyl carrier protein ligase DltA from Bacillus cereus.
Biochemistry
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