UDP-N-acetylmuramoylalanine--D-glutamate ligase (P14900)

Identification
Name:UDP-N-acetylmuramoylalanine--D-glutamate ligase
Synonyms:
  • D-glutamic acid-adding enzyme
  • UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Gene Name:murD
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0D-Glutamic acid + 1.0UDP-N-Acetylmuramoyl-L-alanine ↔ 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate + 1.0UDP-N-Acetylmuramoyl-L-alanyl-D-glutamate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0UDP-N-Acetylmuramoyl-L-alanine + 1.0D-Glutamic acid ↔ 1.0ADP + 1.0Phosphate + 1.0UDP-N-Acetylmuramoyl-L-alanyl-D-glutamate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0UDP-N-acetylmuramoyl-L-alanyl-D-glutamate+1.0Thumb+1.0Thumb
1.0UDP-N-Acetylmuramoyl-L-alanine + 1.0Adenosine triphosphate + 1.0D-Glutamic acid → 1.0Adenosine diphosphate + 1.0Phosphate + 1.0UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + 1.0ADP + 1.0UDP-N-Acetylmuramoyl-L-alanyl-D-glutamate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0UDP-N-Acetylmuramyl-L-Ala + 1.0Adenosine triphosphate + 1.0D-Glutamic acid → 1.0UDP-N-Acetylmuramoyl-L-alanyl-D-glutamate + 1.0ADP + 1.0Phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0D-Glutamic acid + 1.0UDP-N-Acetylmuramoyl-L-alanine ↔ 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate + 1.0UDP-N-Acetylmuramoyl-L-alanyl-D-glutamate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Glutamic acid + 1.0UDP-N-Acetylmuramoyl-L-alanine + 1.0Adenosine triphosphate → 1.0Hydrogen ion + 1.0UDP-N-Acetylmuramoyl-L-alanyl-D-glutamate + 1.0Phosphate + 1.0ADP
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB03339D-Glutamic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB04168UDP-N-Acetylmuramoyl-L-alanineMetaboCard
ECMDB04169UDP-N-Acetylmuramoyl-L-alanyl-D-glutamateMetaboCard
ECMDB20485UDP-N-Acetylmuramyl-L-AlaMetaboCard
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
UDP-N-acetylmuramoylalanine-D-glutamate ligase activity
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:b0088
Gene OrientationClockwise
Centisome Percentage:2.09
Left Sequence End97087
Right Sequence End98403
Gene Sequence:
>1317 bp
ATGGCTGATTATCAGGGTAAAAATGTCGTCATTATCGGCCTGGGCCTCACCGGGCTTTCC
TGCGTGGACTTTTTCCTCGCTCGCGGTGTGACGCCGCGCGTTATGGATACGCGTATGACA
CCGCCTGGCCTGGATAAATTACCCGAAGCCGTAGAACGCCACACGGGCAGTCTGAATGAT
GAATGGCTGATGGCGGCAGATCTGATTGTCGCCAGTCCCGGTATTGCACTGGCGCATCCA
TCCTTAAGCGCTGCCGCTGATGCCGGAATCGAAATCGTTGGCGATATCGAGCTGTTCTGT
CGCGAAGCACAAGCACCGATTGTGGCGATTACCGGTTCTAACGGCAAAAGCACGGTCACC
ACGCTAGTGGGTGAAATGGCGAAAGCGGCGGGGGTTAACGTTGGTGTGGGTGGCAATATT
GGCCTGCCTGCGTTGATGCTACTGGATGATGAGTGTGAACTGTACGTGCTGGAACTGTCG
AGCTTCCAGCTGGAAACCACCTCCAGCTTACAGGCGGTAGCAGCGACCATTCTGAACGTG
ACTGAAGATCATATGGATCGCTATCCGTTTGGTTTACAACAGTATCGTGCAGCAAAACTG
CGCATTTACGAAAACGCGAAAGTTTGCGTGGTTAATGCTGATGATGCCTTAACAATGCCG
ATTCGCGGTGCGGATGAACGCTGCGTCAGCTTTGGCGTCAACATGGGTGACTATCACCTG
AATCATCAGCAGGGCGAAACCTGGCTGCGGGTTAAAGGCGAGAAAGTGCTGAATGTGAAA
GAGATGAAACTTTCCGGGCAGCATAACTACACCAATGCGCTGGCGGCGCTGGCGCTGGCA
GATGCTGCAGGGTTACCGCGTGCCAGCAGCCTGAAAGCGTTAACCACATTCACTGGTCTG
CCGCATCGCTTTGAAGTTGTGCTGGAGCATAACGGCGTACGTTGGATTAACGATTCGAAA
GCGACCAACGTCGGCAGTACGGAAGCGGCGCTGAATGGCCTGCACGTAGACGGCACACTG
CATTTGTTGCTGGGTGGCGATGGTAAATCGGCGGACTTTAGCCCACTGGCGCGTTACCTG
AATGGCGATAACGTACGTCTGTATTGTTTCGGTCGTGACGGCGCGCAGCTGGCGGCGCTA
CGCCCGGAAGTGGCAGAACAAACCGAAACTATGGAACAGGCGATGCGCTTGCTGGCTCCG
CGTGTTCAGCCGGGCGATATGGTTCTGCTCTCCCCAGCCTGTGCCAGCCTTGATCAGTTC
AAGAACTTTGAACAACGAGGCAATGAGTTTGCCCGTCTGGCGAAGGAGTTAGGTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:438
Protein Molecular Weight:46973
Protein Theoretical pI:5
PDB File:1EEH
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>UDP-N-acetylmuramoylalanine--D-glutamate ligase
MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGSLND
EWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVT
TLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNV
TEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHL
NHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGL
PHRFEVVLEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYL
NGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLLSPACASLDQF
KNFEQRGNEFARLAKELG
References
External Links:
ResourceLink
Uniprot ID:P14900
Uniprot Name:MURD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321969
PDB ID:1EEH
Ecogene ID:EG10620
Ecocyc:EG10620
ColiBase:b0088
Kegg Gene:b0088
EchoBASE ID:EB0615
CCDB:MURD_ECOLI
BacMap:16128081
General Reference:
  • Bertrand, J. A., Auger, G., Fanchon, E., Martin, L., Blanot, D., van Heijenoort, J., Dideberg, O. (1997). "Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli." EMBO J 16:3416-3425. Pubmed: 9218784
  • Bertrand, J. A., Fanchon, E., Martin, L., Chantalat, L., Auger, G., Blanot, D., van Heijenoort, J., Dideberg, O. (2000). ""Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase." J Mol Biol 301:1257-1266. Pubmed: 10966819
  • 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
  • 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
  • Ikeda, M., Sato, T., Wachi, M., Jung, H. K., Ishino, F., Kobayashi, Y., Matsuhashi, M. (1989). "Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively." J Bacteriol 171:6375-6378. Pubmed: 2509435
  • Ikeda, M., Wachi, M., Ishino, F., Matsuhashi, M. (1990). "Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli." Nucleic Acids Res 18:1058. Pubmed: 2179861
  • Mengin-Lecreulx, D., van Heijenoort, J. (1990). "Nucleotide sequence of the murD gene encoding the UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli." Nucleic Acids Res 18:183. Pubmed: 2129548
  • Pratviel-Sosa, F., Mengin-Lecreulx, D., van Heijenoort, J. (1991). "Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli." Eur J Biochem 202:1169-1176. Pubmed: 1765076
  • 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