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Information on EC 2.7.1.195 - protein-Npi-phosphohistidine-2-O-alpha-mannosyl-D-glycerate phosphotransferase and Organism(s) Escherichia coli and UniProt Accession P54745

for references in articles please use BRENDA:EC2.7.1.195
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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.
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This record set is specific for:
Escherichia coli
UNIPROT: P54745
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-O-alpha-mannosyl-D-glycerate PTS permease, EC 2.7.1.69, EIImannosylglycerate, EIIMngA, Frx, HrsA, IIHrsA, IIMngA, mngA, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-O-alpha-mannosyl-D-glycerate PTS permease
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EIImannosylglycerate
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EIIMngA
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Frx
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IIHrsA
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IIMngA
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mngA
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SYSTEMATIC NAME
IUBMB Comments
protein-Npi-phospho-L-histidine:2-O-alpha-mannopyranosyl-D-glycerate 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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[protein]-Npi-phospho-L-histidine + 2-O-alpha-mannosyl-D-glycerate [side 1]
[protein]-L-histidine + 2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate [side 2]
show the reaction diagram
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[protein]-Npi-phospho-L-histidine + 2-O-alpha-mannosyl-D-glycerate [side 1]
[protein]-L-histidine + 2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate [side 2]
show the reaction diagram
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
2-O-alpha-mannosyl-D-glycerate [side 1]
apparent value, at pH 7.6, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
deletion of mngR results in the up-regulation of the gene mngA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sampaio, M.; Chevance, F.; Dippel, R.; Eppler, T.; Schlegel, A.; Boos, W.; Lu, Y.; Rock, C.
Phosphotransferase-mediated transport of the osmolyte 2-O-alpha-mannosyl-D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA) gene and is regulated by the mngR (farR) gene product acting as repressor
J. Biol. Chem.
279
5537-5548
2004
Escherichia coli (P54745)
Manually annotated by BRENDA team