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EC Tree
IUBMB Comments This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
The enzyme appears in viruses and cellular organisms
Synonyms
enzyme iinag, eii permease, enzyme iin-acetylglucosamine,
cbe4532 , eiinag, glcnac-specific enzyme ii, glcnac pts, enzyme ii specific for n-acetylglucosamine,
more
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EC 2.7.1.69
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formerly, part transferred
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enzyme II specific for N-acetylglucosamine
enzyme IIN-acetylglucosamine
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GlcNAc 6-P deacetylase
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GlcNAc-specific enzyme II
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GlcNAc-specific phosphotransferase system transporter
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GlcNAc6P-specific transporter of the GlcNAc PTS
N-acetyl-D-glucosamine PTS permease
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N-acetylglucosamine-specific transporter nNag
phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system
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cbe4532
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EIICBANag
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EIINag
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enzyme II specific for N-acetylglucosamine
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enzyme II specific for N-acetylglucosamine
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enzyme II specific for N-acetylglucosamine
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enzyme IInag
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GlcNAc PTS
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GlcNAc6P-specific transporter of the GlcNAc PTS
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GlcNAc6P-specific transporter of the GlcNAc PTS
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N-acetylglucosamine-specific transporter nNag
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N-acetylglucosamine-specific transporter nNag
Vibrio cholerae serotype O1 non-O1 1148A
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nagE
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nagE
Vibrio cholerae serotype O1 non-O1 1148A
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1] = [protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side 2]
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
protein-Npi-phospho-L-histidine:N-acetyl-D-glucosamine Npi-phosphotransferase
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
Vibrio cholerae serotype O1 non-O1 1148A
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
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[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine[side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side2]
Vibrio cholerae serotype O1 non-O1 1148A
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additional information
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not inhibited by chitobiose
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brenda
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brenda
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UniProt
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UniProt
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brenda
Vibrio cholerae serotype O1 non-O1 1148A
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brenda
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brenda
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UniProt
brenda
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brenda
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metabolism
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the nagE-encoded enzyme makes an important contribution to the recycling of peptidoglycan
metabolism
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the nagE-encoded enzyme makes an important contribution to the recycling of peptidoglycan
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65000
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x * 65000, SDS-PAGE
68700
x * 68700, calculated from amino acid sequence
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x * 65000, SDS-PAGE
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x * 68700, calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Corynebacterium glutamicum and Escherichia coli strain LR2-168
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expressed in Escherichia coli IBPC463 cells
expressed in Escherichia coli IBPC590 cells
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expressed in Escherichia coli JW0665-1 cells
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expressed in Escherichia coli strain JM109
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protein NagC represses the enzyme expression
transcriptionally induced in the presence of N-acetylglucosamine and cAMP
transcriptionally induced in the presence of N-acetylglucosamine and cAMP
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transcriptionally induced in the presence of N-acetylglucosamine and cAMP
Vibrio cholerae serotype O1 non-O1 1148A
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Peri, K.G.; Waygood, E.B.
Sequence of cloned enzyme IIN-acetylglucosamine of the phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system of Escherichia coli
Biochemistry
27
6054-6061
1988
Escherichia coli
brenda
Plumbridge, J.
An alternative route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in Escherichia coli
J. Bacteriol.
191
5641-5647
2009
Escherichia coli, Escherichia coli JW0662
brenda
Al Makishah, N.H.; Mitchell, W.J.
Dual substrate specificity of an N-acetylglucosamine phosphotransferase system in Clostridium beijerinckii
Appl. Environ. Microbiol.
79
6712-6718
2013
Clostridium beijerinckii, Clostridium beijerinckii NCIMB8052
brenda
Matano, C.; Uhde, A.; Youn, J.W.; Maeda, T.; Clermont, L.; Marin, K.; Kraemer, R.; Wendisch, V.F.; Seibold, G.M.
Engineering of Corynebacterium glutamicum for growth and L-lysine and lycopene production from N-acetyl-glucosamine
Appl. Microbiol. Biotechnol.
98
5633-5643
2014
Corynebacterium glyciniphilum
brenda
Yamano, N.; Oura, N.; Wang, J.; Fujishima, S.
Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae Non-O1
Biosci. Biotechnol. Biochem.
61
1349-1353
1997
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 non-O1 1148A
brenda
Rogers, M.J.; Ohgi, T.; Plumbridge, J.; Soell, D.
Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase
Gene
62
197-207
1988
Escherichia coli (P09323), Escherichia coli
brenda
Vogler, A.P.; Lengeler, J.W.
Comparison of the sequences of the nagE operons from Klebsiella pneumoniae and Escherichia coli K12: enhanced variability of the enzyme IIN-acetylglucosamine in regions connecting functional domains
Mol. Gen. Genet.
230
270-276
1991
Escherichia coli (P09323), Klebsiella pneumoniae (P45604), Klebsiella pneumoniae, Klebsiella pneumoniae KAY2051 (P45604)
brenda
Plumbridge, J.
DNA binding sites for the Mlc and NagC proteins: regulation of nagE, encoding the N-acetylglucosamine-specific transporter in Escherichia coli
Nucleic Acids Res.
29
506-514
2001
Escherichia coli (P09323)
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