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[IIA-FPr diphosphoryl transfer protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[IIA-FPr diphosphoryl transfer protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]

[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]

[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[IIA-FPr diphosphoryl transfer protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[IIA-FPr diphosphoryl transfer protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]

[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]

[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction

-
enzyme gene frwC deletion can enhance biofilm formation and capsular polysaccharide biosynthesis but decreases the growth rate and lethality in mice
malfunction
-
enzyme gene frwC deletion can enhance biofilm formation and capsular polysaccharide biosynthesis but decreases the growth rate and lethality in mice
-
metabolism

-
the inducible fructose permease is also responsible for xylitol transport
metabolism
-
the utilization of fructose occurs via Enzyme IIfru and FPr protein at fructose concentrations higher than 2.5 mM
metabolism
-
the inducible fructose permease is also responsible for xylitol transport
-
physiological function

Q8DWE7; Q8DWE6
FruCD/inducible fructose permeaseFruI double mutants have roughly 30% of the capacity of the wild-type strain to transport fructose via the phosphoenolpyruvate-dependent sugar:phosphotransferase system
physiological function
-
frwC gene expression is controlled by cyclic AMP receptor protein directly and that such regulation contributes to bacterial growth, capsular polysaccharide synthesis, and the virulence of the cyclic AMP receptor protein-deficient strain
physiological function
-
frwC gene expression is controlled by cyclic AMP receptor protein directly and that such regulation contributes to bacterial growth, capsular polysaccharide synthesis, and the virulence of the cyclic AMP receptor protein-deficient strain
-
physiological function
-
FruCD/inducible fructose permeaseFruI double mutants have roughly 30% of the capacity of the wild-type strain to transport fructose via the phosphoenolpyruvate-dependent sugar:phosphotransferase system
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Schauder, S.; Nunn, R.S.; Lanz, R.; Erni, B.; Schirmer, T.
Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilis
J. Mol. Biol.
276
591-602
1998
Bacillus subtilis
brenda
Durham, D.R.; Phibbs, P.V.
Fractionation and characterization of the phosphoenolpyruvate: fructose 1-phosphotransferase system from Pseudomonas aeruginosa
J. Bacteriol.
149
534-541
1982
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO
brenda
Waygood, E.
Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components; enzyme II(fructose) and fructose-induced HPr-like protein (FPr)
Can. J. Biochem.
58
1144-1146
1980
Escherichia coli
brenda
Lolkema, J.S.; ten Hoeve-Duurkens, R.H.; Robillard, G.T.
The phosphoenolpyruvate-dependent fructose-specific phosphotransferase system in Rhodopseudomonas sphaeroides. EIIFru possesses a Zn2+-binding site and a dithiol/disulfide redox centre
Eur. J. Biochem.
154
651-656
1986
Cereibacter sphaeroides
brenda
Lolkema, J.S.; ten Hoeve-Duurkens, R.H.; Robillard, G.T.
The phosphoenolpyruvate-dependent fructose-specific phosphotransferase system in Rhodopseudomonas sphaeroides. Distribution of EIIFru over the membranes of phototrophically grown Rps. sphaeroides
Eur. J. Biochem.
161
211-215
1986
Cereibacter sphaeroides
brenda
Kornberg, H.
The roles of HPr and FPr in the utilization of fructose by Escherichia coli
FEBS Lett.
194
12-15
1986
Escherichia coli
brenda
Wen, Z.; Browngardt, C.; Burne, R.
Characterization of two operons that encode components of fructose-specific enzyme II of the sugar:phosphotransferase system of Streptococcus mutans
FEMS Microbiol. Lett.
205
337-342
2001
Streptococcus mutans, Streptococcus mutans serotype c (Q8DWE7 and Q8DWE6), Streptococcus mutans serotype c UA159 (Q8DWE7 and Q8DWE6), Streptococcus mutans UA159
brenda
Nothaft, H.; Parche, S.; Kamionka, A.; Titgemeyer, F.
In vivo analysis of HPr reveals a fructose-specific phosphotransferase system that confers high-affinity uptake in Streptomyces coelicolor
J. Bacteriol.
185
929-937
2003
Streptomyces coelicolor, Streptomyces coelicolor A3(2) M145
brenda
Charbit, A.; Reizer, J.; Saier, M.H.
Function of the duplicated IIB domain and oligomeric structure of the fructose permease of Escherichia coli
J. Biol. Chem.
271
9997-10003
1996
Escherichia coli
brenda
Prior, T.; Kornberg, H.
Nucleotide sequence of fruA, the gene specifying enzyme IIfru of the phosphoenolpyruvate-dependent sugar phosphotransferase system in Escherichia coli K12
J. Gen. Microbiol.
134
2757-2768
1988
Escherichia coli, no activity in Escherichia coli strain TP28, no activity in Escherichia coli strain TP32, no activity in Escherichia coli strain HK1112, Escherichia coli HK881, Escherichia coli HK994
brenda
de Crecy-Lagard, V.; Binet, M.; Danchin, A.
Fructose phosphotransferase system of Xanthomonas campestris pv. campestris: characterization of the fruB gene
Microbiology
141 (Pt 9)
2253-2260
1995
Xanthomonas campestris, Xanthomonas campestris XC1504
brenda
Reizer, J.; Reizer, A.; Saier, M.H.
Novel phosphotransferase system genes revealed by bacterial genome analysis - a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system
Microbiology
141
961-971
1995
Escherichia coli
brenda
Geerse, R.; Ruig, C.; Schuitema, A.; Postma, P.
Relationship between pseudo-HPr and the PEP: fructose phosphotransferase system in Salmonella typhimurium and Escherichia coli
Mol. Gen. Genet.
203
435-444
1986
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Geerse, R.; Izzo, F.; Postma, P.
The PEP: fructose phosphotransferase system in Salmonella typhimurium: FPr combines Enzyme IIIFru and pseudo-HPr activities
Mol. Gen. Genet.
216
517-525
1989
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
de Crecy-Lagard, V.; Lejeune, P.; Bouvet, O.M.; Danchin, A.
Identification of two fructose transport and phosphorylation pathways in Xanthomonas campestris pv. campestris
Mol. Gen. Genet.
227
465-472
1991
Xanthomonas campestris, Xanthomonas campestris XC1503
brenda
Bolshakova, T.; Molchanova, M.; Erlagaeva, R.; Grigorenko, Y.; Gershanovitch, V.
A novel mutation FruS, altering synthesis of components of the phosphoenolpyruvate: fructose phosphotransferase system in Escherichia coli K12
Mol. Gen. Genet.
232
394-398
1992
Escherichia coli
brenda
Lin, D.; Fan, J.; Wang, J.; Liu, L.; Xu, L.; Li, F.; Yang, J.; Li, B.
The fructose-specific phosphotransferase system of Klebsiella pneumoniae is regulated by global regulator CRP and linked to virulence and growth
Infect. Immun.
86
e00340-18
2018
Klebsiella pneumoniae, Klebsiella pneumoniae NTUH-2044
brenda