UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Details

Name
UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Synonyms
  • 2.5.1.7
  • Enoylpyruvate transferase
  • EPT
  • murZ
  • UDP-N-acetylglucosamine enolpyruvyl transferase
Gene Name
murA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0018954|UDP-N-acetylglucosamine 1-carboxyvinyltransferase
MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQL
GAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGAR
PVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTIMCAATLAEGTT
IIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLV
AAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHP
AFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKL
SGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE
Number of residues
419
Molecular Weight
44817.24
Theoretical pI
6.07
GO Classification
Functions
UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
Processes
cell cycle / cell division / cell wall organization / peptidoglycan biosynthetic process / regulation of cell shape / UDP-N-acetylgalactosamine biosynthetic process
Components
cytosol
General Function
Udp-n-acetylglucosamine 1-carboxyvinyltransferase activity
Specific Function
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic fosfomycin.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0018955|UDP-N-acetylglucosamine 1-carboxyvinyltransferase (murA)
ATGGATAAATTTCGTGTTCAGGGGCCAACGAAGCTCCAGGGCGAAGTCACAATTTCCGGC
GCTAAAAATGCTGCTCTGCCTATCCTTTTTGCCGCACTACTGGCGGAAGAACCGGTAGAG
ATCCAGAACGTCCCGAAACTGAAAGACGTCGATACATCAATGAAGCTGCTAAGCCAGCTG
GGTGCGAAAGTAGAACGTAATGGTTCTGTGCATATTGATGCCCGCGACGTTAATGTATTC
TGCGCACCTTACGATCTGGTTAAAACCATGCGTGCTTCTATCTGGGCGCTGGGGCCGCTG
GTAGCGCGCTTTGGTCAGGGGCAAGTTTCACTACCTGGCGGTTGTACGATCGGTGCGCGT
CCGGTTGATCTACACATTTCTGGCCTCGAACAATTAGGCGCGACCATCAAACTGGAAGAA
GGTTACGTTAAAGCTTCCGTCGATGGTCGTTTGAAAGGTGCACATATCGTGATGGATAAA
GTCAGCGTTGGCGCAACGGTGACCATCATGTGTGCTGCAACCCTGGCGGAAGGCACCACG
ATTATTGAAAACGCAGCGCGTGAACCGGAAATCGTCGATACCGCGAACTTCCTGATTACG
CTGGGTGCGAAAATTAGCGGTCAGGGCACCGATCGTATCGTCATCGAAGGTGTGGAACGT
TTAGGCGGCGGTGTCTATCGCGTTCTGCCGGATCGTATCGAAACCGGTACTTTCCTGGTG
GCGGCGGCGATTTCTCGCGGCAAAATTATCTGCCGTAACGCGCAGCCAGATACTCTCGAC
GCCGTGCTGGCGAAACTGCGTGACGCTGGAGCGGACATCGAAGTCGGCGAAGACTGGATT
AGCCTGGATATGCATGGCAAACGTCCGAAGGCTGTTAACGTACGTACCGCGCCGCATCCG
GCATTCCCGACCGATATGCAGGCCCAGTTCACGCTGTTGAACCTGGTGGCAGAAGGGACC
GGGTTTATCACCGAAACGGTCTTTGAAAACCGCTTTATGCATGTGCCAGAGCTGAGCCGT
ATGGGCGCGCACGCCGAAATCGAAAGCAATACCGTTATTTGTCACGGTGTTGAAAAACTT
TCTGGCGCACAGGTTATGGCAACCGATCTGCGTGCATCAGCAAGCCTGGTGCTGGCTGGC
TGTATTGCGGAAGGGACGACGGTGGTTGATCGTATTTATCACATCGATCGTGGCTACGAA
CGCATTGAAGACAAACTGCGCGCTTTAGGTGCAAATATTGAGCGTGTGAAAGGCGAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A749
UniProtKB Entry NameMURA_ECOLI
GenBank Protein ID146902
GenBank Gene IDM92358
General References
  1. Marquardt JL, Siegele DA, Kolter R, Walsh CT: Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase. J Bacteriol. 1992 Sep;174(17):5748-52. [Article]
  2. Horii T, Kimura T, Sato K, Shibayama K, Ohta M: Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26. Antimicrob Agents Chemother. 1999 Apr;43(4):789-93. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Mutschler H, Gebhardt M, Shoeman RL, Meinhart A: A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis. PLoS Biol. 2011 Mar;9(3):e1001033. doi: 10.1371/journal.pbio.1001033. Epub 2011 Mar 22. [Article]
  6. Skarzynski T, Mistry A, Wonacott A, Hutchinson SE, Kelly VA, Duncan K: Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure. 1996 Dec 15;4(12):1465-74. [Article]
  7. Skarzynski T, Kim DH, Lees WJ, Walsh CT, Duncan K: Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA. Biochemistry. 1998 Feb 24;37(8):2572-7. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00828FosfomycinapprovedyesinhibitorDetails