CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.470 | D-amino Acid Aminotransferase; Chain A, domain 1 |
|
3.30.470.20 | ATP-grasp fold, B domain |
Domain Context
CATH Clusters
| Superfamily | ATP-grasp fold, B domain |
| Functional Family | D-alanine-D-X ligase VanD4 |
Enzyme Information
| 6.1.2.1 |
D-alanine--(R)-lactate ligase.
based on mapping to UniProt P25051
D-alanine + (R)-lactate + ATP = D-alanyl-(R)-lactate + ADP + phosphate.
-!- The product of this enzyme, the depsipeptide D-alanyl-(R)-lactate, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4. -!- The resulting peptidoglycan does not bind the glycopeptide antibiotics vancomycin and teicoplanin, conferring resistance on the bacteria.
|
| 6.3.2.4 |
D-alanine--D-alanine ligase.
based on mapping to UniProt P25051
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.
-!- Involved with EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide.
|
UniProtKB Entries (1)
| P25051 |
VANA_ENTFC
Enterococcus faecium
Vancomycin/teicoplanin A-type resistance protein VanA
|
PDB Structure
| PDB | 1E4E |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA).
Proc. Natl. Acad. Sci. U.S.A.
|