2.7.8.13	dansyl-UDP-NAc-muramoyl-pentapeptide + undecaprenyl phosphate	-	Escherichia coli	UMP + dansyl-UDP-NAc-muramoyl-pentapeptide-diphosphoundecaprenol	-	?	452451	
2.7.8.13	additional information	catalyzes an exchange reaction between UMP and UDP-MurNAc-pentapeptide in the absence of undecaprenyl phosphate	Staphylococcus aureus	?	-	?	89	
2.7.8.13	additional information	catalyzes an exchange reaction between UMP and UDP-MurNAc-pentapeptide in the absence of undecaprenyl phosphate	Escherichia coli	?	-	?	89	
2.7.8.13	additional information	all five cytoplasmic segments contribute to catalytic site with at least 14 invariant polar and/or charged, non-clustered residues, conserved residue D98 supposedly involved in deprotonation of lipid substrate during catalysis at physiological pH 7.4 (pKa for undecaprenyl phosphate: 6.6 and 9.2)	Bacillus subtilis	?	-	?	89	
2.7.8.13	additional information	functional complementation in a MraY-lacking, thermosensitive Escherichia coli mutant strain (2fold increased UDP-N-acetylmuramoyl-pentapeptide level compared to wild-type cells when grown 30 min at 42°C, depletion of lipid I) by overexpression of wild-type or mutants E299Q, D177N, N168A, H45R, K48Q, H291R	Bacillus subtilis	?	-	?	89	
2.7.8.13	additional information	UDP-N-acetylmuramyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine: Park’s nucleotide, UDP-MurNAc-pentapeptide	Bacteria	?	-	?	89	
2.7.8.13	additional information	assay method development for high-throughput screening assays and metadata annotation, overview	Bacillus subtilis	?	-	?	89	
2.7.8.13	additional information	the enzyme does not display any diphosphatase activity on the nucleotide substrate. No activity with UDP-GlcNAc and 1-diphospho-MurNAc-pentapeptide. Enzyme catalytic mechanism and substrate specificity, overview. The essential aspartate residue, that is invariant in the superfamily, is Asp98 in Bacillus subtilis MraY, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. UDPMurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-Ala-D-Glu and UDPMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate precursors of the peptidoglycan biosynthesis pathway are all substrates of the enzyme, no activity with 1-diphospho-MurNAc-pentapeptide. No activity with isopentenyl phosphate as lipid substrate, the enzyme is highly active when tested with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate	Bacillus subtilis	?	-	?	89	
2.7.8.13	additional information	assay method development for high-throughput screening assays and metadata annotation, overview	Bacillus subtilis 168	?	-	?	89	
2.7.8.13	additional information	the enzyme does not display any diphosphatase activity on the nucleotide substrate. No activity with UDP-GlcNAc and 1-diphospho-MurNAc-pentapeptide. Enzyme catalytic mechanism and substrate specificity, overview. The essential aspartate residue, that is invariant in the superfamily, is Asp98 in Bacillus subtilis MraY, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. UDPMurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-Ala-D-Glu and UDPMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate precursors of the peptidoglycan biosynthesis pathway are all substrates of the enzyme, no activity with 1-diphospho-MurNAc-pentapeptide. No activity with isopentenyl phosphate as lipid substrate, the enzyme is highly active when tested with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate	Bacillus subtilis 168	?	-	?	89