Homologous Superfamily

Mur-like, catalytic domain superfamily (IPR036565)

Short name: Mur-like_cat_sf

Overlapping entries


Mur ligases play an essential role in the intracellular biosynthesis of bacterial peptidoglycan. Mur ligases share the same three-domain topology, with N-terminal and central domains responsible for binding the UDP-precursor and ATP, respectively, while the C-terminal part binds the condensing amino acid residue [PMID: 17507028].

This superfamily represents the central domain from all four Mur enzymes: UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanine-D-glutamate ligase (MurD), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). It also includes folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate and cyanophycin synthetase that catalyses the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin) [PMID: 9652408].

GO terms

Biological Process

GO:0009058 biosynthetic process

Molecular Function

GO:0005524 ATP binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.