Information on EC 2.7.1.202 - protein-Npi-phosphohistidine-D-fructose phosphotransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.202
-
RECOMMENDED NAME
GeneOntology No.
protein-Npi-phosphohistidine-D-fructose phosphotransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[protein]-Npi-phospho-L-histidine + D-fructose[side 1] = [protein]-L-histidine + D-fructose 1-phosphate[side 2]
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-Npi-phospho-L-histidine:D-fructose 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 usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli strain HK1112
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli strain TP28
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli strain TP32
-
-
-
Manually annotated by BRENDA team
Q8DWE7 encodes domains BC, Q8DWE6 encodes domain A of phosphoenolpyruvate-dependent fructose:phosphotransferase system, respectively
Q8DWE7 and Q8DWE6
UniProt
Manually annotated by BRENDA team
Q8DWE7 encodes domains BC, Q8DWE6 encodes domain A of phosphoenolpyruvate-dependent fructose:phosphotransferase system, respectively
Q8DWE7 and Q8DWE6
UniProt
Manually annotated by BRENDA team
pv. campestris
-
-
Manually annotated by BRENDA team
pv. campestris
-
-
Manually annotated by BRENDA team
pv. campestris
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[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]
show the reaction diagram
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[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]
show the reaction diagram
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein HPr]-L-histidine + D-fructose 1-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 1-phosphate[side 2]
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
Zn2+
-
contains zinc
additional information
-
metal ions are not required for the exchange activity of the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ferricyanide
-
addition of 0.2 mM ferricyanide causes a rapid oxidation of the enzyme
N-ethylmaleimide
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dithiol
-
essential for activity
fructose-induced HPr-like protein
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
D-fructose[side 1]
-
at pH 7.4 and 32°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18494
-
x * 18494, subunit IIBLev with six selenomethionines, electrospray mass spectroscopy
57500
-
x * 57500, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IIB subunit, hanging drop vapor diffusion method, using 3.2-3.8 M sodium formate, 0.1 M Tris, pH 9.0
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
binding of zinc to or phosphorylating the enzyme protects it against trypsin inactivation
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli D41 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is inducible by sucrose and fructose
the level of the fruA transcript is 3-4fold higher in D-fructose-grown mycelia compared to glycerol or D-glucose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C112S
-
inactive