Sequence of GLMU_ECOLI
EC Number:2.3.1.157
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Other sequences found for EC No. 2.3.1.157
EC Number:2.7.7.23
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
UDP-N-acetylglucosamine diphosphorylase
P0ACC7
Escherichia coli (strain K12)
456
49190
Reaction
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Other sequences found for EC No. 2.7.7.23
General information:
Sequence
0 MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH VHLVYGHGGD
60 LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL MLYGDVPLIS VETLQRLRDA
120 KPQGGIGLLT VKLDDPTGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM
180 KRWLAKLTNN NAQGEYYITD IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ
240 SEQAEKLLLA GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN
300 SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM KKARLGKGSK
360 AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT
420 IAAGTTVTRN VGENALAISR VPQTQKEGWR RPVKKK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
297324
Walker J.E.,Gay N.J.,Saraste M.,Eberle A.N.
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.
224
799-815
1984
297325
Burland V.D.,Plunkett G. III,Daniels D.L.,Blattner F.R.
DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication.
Genomics
16
551-561
1993
297326
Blattner F.R.,Plunkett G. III,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.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
297327
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
297328
Mengin-Lecreulx D.,van Heijenoort J.
Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli.
J. Bacteriol.
175
6150-6157
1993
297329
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.
176
5788-5795
1994
297330
Gehring A.M.,Lees W.J.,Mindiola D.J.,Walsh C.T.,Brown E.D.
Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.
Biochemistry
35
579-585
1996
297331
Pompeo F.,van Heijenoort J.,Mengin-Lecreulx D.
Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes.
J. Bacteriol.
180
4799-4803
1998
297332
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.
18
4096-4107
1999
297333
Olsen L.R.,Roderick S.L.
Structure of the Escherichia coli glmU pyrophosphorylase and acetyltransferase active sites.
Biochemistry
40
1913-1921
2001
297334
Olsen L.R.,Vetting M.W.,Roderick S.L.
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Protein Sci.
16
1230-1235
2007
297335
Buurman E.T.,Andrews B.,Gao N.,Hu J.,Keating T.A.,Lahiri S.,Otterbein L.R.,Patten A.D.,Stokes S.S.,Shapiro A.B.
In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae.
J. Biol. Chem.
286
40734-40742
2011
297336
Green O.M.,McKenzie A.R.,Shapiro A.B.,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-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series.
Bioorg. Med. Chem. Lett.
22
1510-1519
2012
