CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.58 | Methane Monooxygenase Hydroxylase; Chain G, domain 1 |
|
1.20.58.90 |
Domain Context
CATH Clusters
| Superfamily | 1.20.58.90 |
| Functional Family |
Enzyme Information
| 2.3.2.17 |
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N(6)-glycyl)-D-alanyl-D- alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase.
based on mapping to UniProt P0A0A5
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-Gly)-D-Ala-D-Ala-diphospho- ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNA = MurNAc-L-Ala-D- isoglutaminyl-L-Lys-(N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis- undecaprenyl-GlcNAc + 2 tRNA.
-!- This enzyme catalyzes the successive transfer of two glycine moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-Gly)- D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc, attaching them to a glycine residue previously attached by EC 2.3.2.16 (FemX) to the N(6) of the L-lysine at position 3 of the pentapeptide. -!- This is the second step in the synthesis of the pentaglycine interpeptide bridge that is used by Staphylococcus aureus for the crosslinking of different glycan strands to each other. -!- The next step is catalyzed by EC 2.3.2.18 (FemB). -!- This enzyme is essential for methicillin resistance.
|
UniProtKB Entries (1)
| P0A0A5 |
FEMA_STAAU
Staphylococcus aureus
Aminoacyltransferase FemA
|
PDB Structure
| PDB | 1LRZ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
X-ray crystal structure of Staphylococcus aureus FemA.
Structure
|
