Mur-like, catalytic domain superfamily (IPR036565)
Short name: Mur-like_cat_sf
- Folylpolyglutamate synthetase (IPR001645)
- Murein peptide ligase (IPR005757)
- UDP-N-acetylmuramate--L-alanine ligase (IPR005758)
- UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (IPR005761)
- UDP-N-acetylmuramoylalanine-D-glutamate ligase (IPR005762)
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase (IPR005863)
- Capsule biosynthesis protein CapB (IPR008337)
- Mur ligase, central (IPR013221)
- Folylpolyglutamate synthetase, conserved site (IPR018109)
- Folylpolyglutamate synthase, eukaryota (IPR023600)
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].