CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.630.30
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.
Benson, T.E., Prince, D.B., Mutchler, V.T., Curry, K.A., Ho, A.M., Sarver, R.W., Hagadorn, J.C., Choi, G.H., Garlick, R.L.
Structure
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