Bifunctional protein GlmU

Details

Name
Bifunctional protein GlmU
Synonyms
  • yieA
Gene Name
glmU
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0004003|Bifunctional protein GlmU
MLNNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHLVYGHGGD
LLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDA
KPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADM
KRWLAKLTNNNAQGEYYITDIIALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQ
SEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKN
SVIGDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSK
AGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGAT
IAAGTTVTRNVGENALAISRVPQTQKEGWRRPVKKK
Number of residues
456
Molecular Weight
49189.765
Theoretical pI
6.52
GO Classification
Functions
glucosamine-1-phosphate N-acetyltransferase activity / identical protein binding / magnesium ion binding / UDP-N-acetylglucosamine diphosphorylase activity
Processes
cell morphogenesis / cell wall organization / lipid A biosynthetic process / lipopolysaccharide biosynthetic process / peptidoglycan biosynthetic process / regulation of cell shape / UDP-N-acetylglucosamine biosynthetic process
Components
cytosol
General Function
Udp-n-acetylglucosamine diphosphorylase activity
Specific Function
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0021318|Bifunctional protein GlmU (glmU)
ATGTTGAATAATGCTATGAGCGTAGTGATCCTTGCCGCAGGCAAAGGCACGCGCATGTAT
TCCGATCTTCCGAAAGTGCTGCATACCCTTGCCGGGAAAGCGATGGTTCAGCATGTCATT
GATGCTGCGAATGAATTAGGCGCAGCGCACGTTCACCTGGTGTACGGTCACGGCGGCGAT
CTGCTAAAACAGGCGCTGAAAGACGACAACCTTAACTGGGTGCTTCAGGCAGAGCAGCTG
GGTACGGGTCATGCAATGCAGCAGGCCGCACCTTTCTTTGCCGATGATGAAGACATTTTA
ATGCTCTACGGCGACGTGCCGCTGATCTCTGTCGAAACACTCCAGCGTCTGCGTGATGCT
AAACCGCAGGGTGGCATTGGTCTGCTGACGGTGAAACTGGATGATCCGACCGGTTATGGA
CGTATCACCCGTGAAAACGGCAAAGTTACCGGCATTGTTGAGCACAAAGATGCCACCGAC
GAGCAGCGTCAGATTCAGGAGATCAACACCGGCATTCTGATTGCCAACGGCGCAGATATG
AAACGCTGGCTGGCGAAGCTGACCAACAATAATGCTCAGGGCGAATACTACATCACCGAC
ATTATTGCGCTGGCGTATCAGGAAGGGCGTGAAATCGTCGCCGTTCATCCGCAACGTTTA
AGCGAAGTAGAAGGCGTGAATAACCGCCTGCAACTCTCCCGTCTGGAGCGTGTTTATCAG
TCCGAACAGGCTGAAAAACTGCTGTTAGCAGGCGTTATGCTGCGCGATCCAGCGCGTTTT
GATCTGCGTGGTACGCTAACTCACGGGCGCGATGTTGAAATTGATACTAACGTTATCATC
GAGGGCAACGTGACTCTCGGTCATCGCGTGAAAATTGGCACCGGTTGCGTGATTAAAAAC
AGCGTGATTGGCGATGATTGCGAAATCAGTCCGTATACCGTTGTGGAAGATGCGAATCTG
GCAGCGGCCTGTACCATTGGCCCGTTTGCCCGTTTGCGTCCTGGTGCTGAGTTGCTGGAA
GGTGCTCACGTCGGTAACTTCGTTGAGATGAAAAAAGCGCGTCTGGGTAAAGGCTCGAAA
GCTGGTCATCTGACTTACCTGGGCGATGCGGAAATTGGCGATAACGTTAACATCGGCGCG
GGAACCATTACCTGCAACTACGATGGTGCGAATAAATTTAAGACCATTATCGGCGACGAT
GTGTTTGTTGGTTCCGACACTCAGCTGGTGGCCCCGGTAACAGTAGGCAAAGGCGCGACC
ATTGCTGCGGGTACAACTGTGACGCGTAATGTCGGCGAAAATGCATTAGCTATCAGCCGT
GTGCCGCAGACTCAGAAAGAAGGCTGGCGTCGTCCGGTAAAGAAAAAGTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0ACC7
UniProtKB Entry NameGLMU_ECOLI
GenBank Gene IDX01631
General References
  1. Walker JE, Gay NJ, Saraste M, Eberle AN: DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS. Biochem J. 1984 Dec 15;224(3):799-815. [Article]
  2. Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. [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. Mengin-Lecreulx D, van Heijenoort J: Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli. J Bacteriol. 1993 Oct;175(19):6150-7. [Article]
  6. Mengin-Lecreulx D, van Heijenoort J: Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J Bacteriol. 1994 Sep;176(18):5788-95. [Article]
  7. Gehring AM, Lees WJ, Mindiola DJ, Walsh CT, Brown ED: Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry. 1996 Jan 16;35(2):579-85. [Article]
  8. Pompeo F, van Heijenoort J, Mengin-Lecreulx D: Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes. J Bacteriol. 1998 Sep;180(18):4799-803. [Article]
  9. Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y: Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. EMBO J. 1999 Aug 2;18(15):4096-107. [Article]
  10. Olsen LR, Roderick SL: Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry. 2001 Feb 20;40(7):1913-21. [Article]
  11. Olsen LR, Vetting MW, Roderick SL: Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Protein Sci. 2007 Jun;16(6):1230-5. Epub 2007 May 1. [Article]
  12. Buurman ET, Andrews B, Gao N, Hu J, Keating TA, Lahiri S, Otterbein LR, Patten AD, Stokes SS, Shapiro AB: In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae. J Biol Chem. 2011 Nov 25;286(47):40734-42. doi: 10.1074/jbc.M111.274068. Epub 2011 Oct 7. [Article]
  13. Green OM, McKenzie AR, Shapiro AB, Otterbein L, Ni H, Patten A, Stokes S, Albert R, Kawatkar S, Breed J: Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetylt ransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series. Bioorg Med Chem Lett. 2012 Feb 15;22(4):1510-9. doi: 10.1016/j.bmcl.2012.01.016. Epub 2012 Jan 14. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails
DB03397Uridine-Diphosphate-N-AcetylglucosamineexperimentalunknownDetails
DB038142-(N-morpholino)ethanesulfonic acidexperimentalunknownDetails