Identification
Name:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
Synonyms:
  • Meso-A2pm-adding enzyme
  • Meso-diaminopimelate-adding enzyme
  • UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
  • UDP-MurNAc-tripeptide synthetase
  • UDP-N-acetylmuramyl-tripeptide synthetase
Gene Name:murE
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0UDP-N-acetylmuramoyl-L-alanyl-D-glutamate+1.0Thumb+1.0Thumb+1.0Thumb1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0meso-diaminopimelate+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01370Diaminopimelic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB21665Meso-2,6-DiaminoheptanedioateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB20203UDP-N-Acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminopimelateMetaboCard
ECMDB04169UDP-N-Acetylmuramoyl-L-alanyl-D-glutamateMetaboCard
ECMDB04170UDP-N-Acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminoheptanedioateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acid-amino acid ligase activity
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
nucleoside binding
purine nucleoside binding
Process
aminoglycan metabolic process
biological regulation
biosynthetic process
carbohydrate metabolic process
cell division
cell wall biogenesis
cell wall organization or biogenesis
cellular cell wall organization or biogenesis
cellular component organization or biogenesis
cellular process
glycosaminoglycan metabolic process
metabolic process
peptidoglycan biosynthetic process
peptidoglycan metabolic process
peptidoglycan-based cell wall biogenesis
polysaccharide metabolic process
primary metabolic process
regulation of biological quality
regulation of cell shape
Gene Properties
Blattner:b0085
Gene OrientationClockwise
Centisome Percentage:2.01
Left Sequence End93166
Right Sequence End94653
Gene Sequence:
>1488 bp
GTGGCAGATCGTAATTTGCGCGACCTTCTTGCTCCGTGGGTGCCAGACGCACCTTCGCGA
GCACTGCGAGAGATGACACTCGACAGCCGTGTGGCTGCGGCGGGCGATCTCTTTGTAGCT
GTAGTAGGTCATCAGGCGGACGGGCGTCGATATATCCCGCAGGCGATAGCGCAAGGTGTG
GCTGCCATTATTGCAGAGGCGAAAGATGAGGCGACCGATGGTGAAATCCGTGAAATGCAC
GGCGTACCGGTCATCTATCTCAGCCAGCTCAACGAGCGTTTATCTGCACTGGCGGGCCGC
TTTTACCATGAACCCTCTGACAATTTACGTCTCGTGGGCGTAACGGGCACCAACGGCAAA
ACCACGACTACCCAGCTGTTGGCGCAGTGGAGCCAACTGCTTGGCGAAATCAGCGCGGTA
ATGGGCACCGTTGGTAACGGCCTGCTGGGGAAAGTGATCCCGACAGAAAATACAACCGGT
TCGGCAGTCGATGTTCAGCATGAGCTGGCGGGGCTGGTGGATCAGGGCGCGACGTTTTGC
GCAATGGAAGTTTCCTCCCACGGGCTGGTACAGCACCGTGTGGCGGCATTGAAATTTGCG
GCGTCGGTCTTTACCAACTTAAGCCGCGATCACCTTGATTATCATGGTGATATGGAACAC
TACGAAGCCGCGAAATGGCTGCTTTATTCTGAGCATCATTGCGGTCAGGCGATTATTAAC
GCCGACGATGAAGTGGGCCGCCGCTGGCTGGCAAAACTGCCGGACGCGGTTGCGGTATCA
ATGGAAGATCATATTAATCCGAACTGTCACGGACGCTGGTTGAAAGCGACCGAAGTGAAC
TATCACGACAGCGGTGCGACGATTCGCTTTAGCTCAAGTTGGGGCGATGGCGAAATTGAA
AGCCATCTGATGGGCGCTTTTAACGTCAGCAACCTGCTGCTCGCGCTGGCGACACTGTTG
GCACTCGGCTATCCACTGGCTGATCTGCTGAAAACCGCCGCGCGTCTGCAACCGGTTTGC
GGACGTATGGAAGTGTTCACTGCGCCAGGCAAACCGACGGTGGTGGTGGATTACGCGCAT
ACGCCGGATGCACTGGAAAAAGCCTTACAGGCGGCGCGTCTGCACTGTGCGGGCAAGCTG
TGGTGTGTCTTTGGCTGTGGTGGCGATCGCGATAAAGGTAAGCGTCCACTGATGGGCGCA
ATTGCCGAAGAGTTTGCTGACGTGGCGGTGGTGACGGACGATAACCCGCGTACCGAAGAA
CCGCGTGCCATCATCAACGATATTCTGGCGGGAATGTTAGATGCCGGACATGCCAAAGTG
ATGGAAGGCCGTGCTGAAGCGGTGACTTGCGCCGTTATGCAGGCTAAAGAGAATGATGTG
GTACTGGTCGCGGGCAAAGGCCATGAAGATTACCAGATTGTTGGCAATCAGCGTCTGGAC
TACTCCGATCGCGTCACGGTGGCGCGTCTGCTGGGGGTGATTGCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:495
Protein Molecular Weight:53343
Protein Theoretical pI:6
PDB File:1E8C
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
MADRNLRDLLAPWVPDAPSRALREMTLDSRVAAAGDLFVAVVGHQADGRRYIPQAIAQGV
AAIIAEAKDEATDGEIREMHGVPVIYLSQLNERLSALAGRFYHEPSDNLRLVGVTGTNGK
TTTTQLLAQWSQLLGEISAVMGTVGNGLLGKVIPTENTTGSAVDVQHELAGLVDQGATFC
AMEVSSHGLVQHRVAALKFAASVFTNLSRDHLDYHGDMEHYEAAKWLLYSEHHCGQAIIN
ADDEVGRRWLAKLPDAVAVSMEDHINPNCHGRWLKATEVNYHDSGATIRFSSSWGDGEIE
SHLMGAFNVSNLLLALATLLALGYPLADLLKTAARLQPVCGRMEVFTAPGKPTVVVDYAH
TPDALEKALQAARLHCAGKLWCVFGCGGDRDKGKRPLMGAIAEEFADVAVVTDDNPRTEE
PRAIINDILAGMLDAGHAKVMEGRAEAVTCAVMQAKENDVVLVAGKGHEDYQIVGNQRLD
YSDRVTVARLLGVIA
References
External Links:
ResourceLink
Uniprot ID:P22188
Uniprot Name:MURE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321966
PDB ID:1E8C
Ecogene ID:EG10621
Ecocyc:EG10621
ColiBase:b0085
Kegg Gene:b0085
EchoBASE ID:EB0616
CCDB:MURE_ECOLI
BacMap:16128078
General Reference:
  • Abo-Ghalia, M., Michaud, C., Blanot, D., van Heijenoort, J. (1985). "Specificity of the uridine-diphosphate-N-acetylmuramyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate synthetase from Escherichia coli." Eur J Biochem 153:81-87. Pubmed: 3905407
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Eveland, S. S., Pompliano, D. L., Anderson, M. S. (1997). "Conditionally lethal Escherichia coli murein mutants contain point defects that map to regions conserved among murein and folyl poly-gamma-glutamate ligases: identification of a ligase superfamily." Biochemistry 36:6223-6229. Pubmed: 9166795
  • Gordon, E., Flouret, B., Chantalat, L., van Heijenoort, J., Mengin-Lecreulx, D., Dideberg, O. (2001). "Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli." J Biol Chem 276:10999-11006. Pubmed: 11124264
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Mengin-Lecreulx, D., Blanot, D., van Heijenoort, J. (1994). "Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli." J Bacteriol 176:4321-4327. Pubmed: 8021219
  • Michaud, C., Mengin-Lecreulx, D., van Heijenoort, J., Blanot, D. (1990). "Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate ligase from Escherichia coli." Eur J Biochem 194:853-861. Pubmed: 2269304
  • Michaud, C., Parquet, C., Flouret, B., Blanot, D., van Heijenoort, J. (1990). "Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli." Biochem J 269:277-278. Pubmed: 2198024
  • Tao, J. S., Ishiguro, E. E. (1989). "Nucleotide sequence of the murE gene of Escherichia coli." Can J Microbiol 35:1051-1054. Pubmed: 2692800
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901