Bifunctional protein glmU (P0ACC7)

Identification
Name:Bifunctional protein glmU
Synonyms:
  • UDP-N-acetylglucosamine pyrophosphorylase
  • N-acetylglucosamine-1-phosphate uridyltransferase
  • Glucosamine-1-phosphate N-acetyltransferase
Gene Name:glmU
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc
Cellular Location:Cytoplasm
SMPDB Pathways:
  • 1,6-anhydro-<i>N</i>-acetylmuramic acid recycling PW002064
  • Amino sugar and nucleotide sugar metabolism I PW000886
  • Lipopolysaccharide biosynthesis PW000831
  • O-antigen building blocks biosynthesis PW002089
  • lipopolysaccharide biosynthesis II PW001905
  • lipopolysaccharide biosynthesis III PW002059
  • peptidoglycan biosynthesis I PW000906
  • peptidoglycan biosynthesis I 2 PW002062
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Uridine triphosphate + 1.0Glucosamine-1P ↔ 1.0Pyrophosphate + 1.0Uridine diphosphate-N-acetylglucosamine
ReactionCard
1.0Thumb+1.0alpha-D-Glucosamine 1-phosphate ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0alpha-D-Glucosamine 1-phosphate ↔ 1.0Coenzyme A + 1.0Glucosamine-1P
ReactionCard
SMPDB Reactions:
1.0Glucosamine-1P+1.0Thumb+1.0Thumb → 1.0N-Acetyl-glucosamine 1-phosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.0Glucosamine-1P + 1.0Acetyl-CoA + 1.0Glucosamine-1P → 1.0N-Acetyl-glucosamine 1-phosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0N-Acetyl-glucosamine 1-phosphate
ReactionCard
1.0N-Acetyl-glucosamine 1-phosphate+1.0Uridine triphosphate+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Pyrophosphate
1.0N-Acetyl-glucosamine 1-phosphate + 1.0Uridine triphosphate + 1.0Hydrogen ion + 1.0N-Acetyl-glucosamine 1-phosphate + 1.0Uridine triphosphate → 1.0Uridine diphosphate-N-acetylglucosamine + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0N-Acetyl-glucosamine 1-phosphate → 1.0N-Acetyl-glucosamine 1-phosphate + 1.0Coenzyme A + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetyl-glucosamine 1-phosphate + 1.0Hydrogen ion + 1.0Uridine triphosphate → 1.0Pyrophosphate + 1.0Uridine diphosphate-N-acetylglucosamine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB21662alpha-D-Glucosamine 1-phosphateMetaboCard
ECMDB21663beta-D-Fructose 2-phosphateMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB01109Glucosamine-1PMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01367N-Acetyl-glucosamine 1-phosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00290Uridine diphosphate-N-acetylglucosamineMetaboCard
ECMDB00285Uridine triphosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acetyltransferase activity
acyltransferase activity
binding
catalytic activity
cation binding
glucosamine-1-phosphate N-acetyltransferase activity
ion binding
magnesium ion binding
metal ion binding
N-acetyltransferase activity
nucleotidyltransferase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
transferase activity, transferring phosphorus-containing groups
UDP-N-acetylglucosamine diphosphorylase activity
uridylyltransferase activity
Process
aminoglycan metabolic process
anatomical structure morphogenesis
biosynthetic process
carbohydrate metabolic process
cell morphogenesis
cellular component morphogenesis
developmental process
glycosaminoglycan metabolic process
lipid biosynthetic process
lipid metabolic process
lipopolysaccharide biosynthetic process
metabolic process
peptidoglycan biosynthetic process
peptidoglycan metabolic process
polysaccharide metabolic process
primary metabolic process
Gene Properties
Blattner:b3730
Gene OrientationCounterclockwise
Centisome Percentage:84.31
Left Sequence End3911853
Right Sequence End3913223
Gene Sequence:
>1371 bp
ATGTTACCTTCTCAATCCCCTGCAATTTTTACCGTTAGTCGCCTGAATCAAACGGTTCGT
CTGCTGCTTGAGCATGAGATGGGACAGGTTTGGATCAGCGGCGAAATTTCTAATTTCACG
CAACCAGCTTCCGGTCACTGGTACTTTACACTCAAAGACGACACCGCCCAGGTACGCTGC
GCGATGTTCCGCAACAGCAACCGCCGGGTGACCTTCCGCCCACAGCATGGGCAACAAGTT
TTAGTTCGCGCCAATATTACGCTCTACGAGCCGCGCGGCGACTACCAGATAATCGTTGAG
AGTATGCAGCCGGCCGGTGAAGGGCTGCTGCAACAGAAGTACGAACAGCTCAAAGCGAAG
TTGCAGGCTGAAGGTTTGTTCGATCAGCAATACAAAAAACCACTTCCCTCCCCTGCGCAT
TGCGTTGGTGTGATCACCTCAAAAACCGGTGCTGCGCTACATGATATTTTGCATGTGTTA
AAACGTCGCGATCCTTCTCTGCCGGTGATCATCTACCCTGCCGCCGTTCAGGGCGATGAC
GCGCCGGGGCAAATTGTTCGCGCCATTGAACTGGCGAATCAGCGCAATGAGTGCGACGTA
TTGATCGTCGGGCGCGGCGGCGGTTCGCTGGAAGATTTATGGAGTTTTAACGACGAACGC
GTAGCGCGGGCGATTTTTACCAGCCGCATTCCGGTTGTCAGCGCCGTCGGGCATGAGACG
GATGTGACCATTGCCGATTTTGTTGCCGATCTGCGTGCGCCAACGCCGTCTGCCGCCGCT
GAAGTAGTGAGCCGTAATCAGCAAGAGTTACTGCGCCAGGTGCAATCGACCCGTCAACGG
CTGGAGATGGCGATGGATTATTATCTCGCCAACCGCACACGTCGCTTTACGCAAATTCAT
CACCGATTACAGCAACAGCATCCGCAGCTCCGGCTGGCACGCCAGCAAACCATGCTTGAG
CGCCTGCAAAAGCGAATGAGCTTTGCGCTGGAAAATCAACTTAAGCGTACCGGGCAACAG
CAGCAGCGGTTAACACAGCGGCTGAATCAGCAAAATCCACAGCCGAAGATTCATCGCGCG
CAAACGCGCATTCAGCAACTGGAATATCGTTTAGCAGAAACCCTGCGCGCACAGCTTAGC
GCCACGCGTGAACGTTTCGGTAATGCAGTAACGCACCTCGAAGCCGTAAGCCCACTGTCA
ACGCTGGCGCGTGGATACAGCGTTACTACTGCTACTGACGGCAATGTACTGAAAAAAGTG
AAGCAAGTTAAAGCGGGTGAAATGCTAACCACACGTCTGGAAGACGGCTGGATAGAAAGT
GAAGTAAAAAACATCCAGCCAGTAAAAAAATCGCGTAAAAAGGTGCATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:456
Protein Molecular Weight:49190
Protein Theoretical pI:7
PDB File:1HV9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Bifunctional protein glmU
MLNNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHLVYGHGGD
LLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDA
KPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADM
KRWLAKLTNNNAQGEYYITDIIALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQ
SEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKN
SVIGDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSK
AGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGAT
IAAGTTVTRNVGENALAISRVPQTQKEGWRRPVKKK
References
External Links:
ResourceLink
Uniprot ID:P0ACC7
Uniprot Name:GLMU_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1805569
PDB ID:1HV9
Ecogene ID:EG11198
Ecocyc:EG11198
ColiBase:b3730
Kegg Gene:b3730
EchoBASE ID:EB1184
CCDB:GLMU_ECOLI
BacMap:16131598
General Reference:
  • 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
  • Brown, K., Pompeo, F., Dixon, S., Mengin-Lecreulx, D., Cambillau, C., Bourne, Y. (1999). "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. Pubmed: 10428949
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Gehring, A. M., Lees, W. J., Mindiola, D. J., Walsh, C. T., Brown, E. D. (1996). "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. Pubmed: 8555230
  • 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., van Heijenoort, J. (1993). "Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli." J Bacteriol 175:6150-6157. Pubmed: 8407787
  • Mengin-Lecreulx, D., van Heijenoort, J. (1994). "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. Pubmed: 8083170
  • Olsen, L. R., Roderick, S. L. (2001). "Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites." Biochemistry 40:1913-1921. Pubmed: 11329257
  • Pompeo, F., van Heijenoort, J., Mengin-Lecreulx, D. (1998). "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 180:4799-4803. Pubmed: 9733680
  • Walker, J. E., Gay, N. J., Saraste, M., Eberle, A. N. (1984). "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. Pubmed: 6395859