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Information on EC 2.7.1.201 - protein-Npi-phosphohistidine-trehalose phosphotransferase and Organism(s) Escherichia coli and UniProt Accession P36672

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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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Escherichia coli
UNIPROT: P36672
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
enzyme iitre, eiitre, trehalose phosphotransferase system, trehalose pts transporter, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enzyme IITre
-
EIITre
trehalose phosphotransferase system
-
-
trehalose PTS permease
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-
-
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trehalose PTS transporter
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trehalose(maltose)-specific PTS system components IIBC
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trehalose-specific enzyme EIICBTre
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-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
protein-Npi-phospho-L-histidine:alpha,alpha-trehalose 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 + alpha,alpha-trehalose[side 1]
[protein]-L-histidine + alpha,alpha-trehalose 6-phosphate[side 2]
show the reaction diagram
enzyme IITre-mediated phosphorylation of trehalose requires the activity of enzyme IIAGlc, a component of the major glucose transport system
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-
?
[protein]-Npi-phospho-L-histidine + alpha,alpha-trehalose[side 1]
[protein]-L-histidine + alpha,alpha-trehalose 6-phosphate[side 2]
show the reaction diagram
additional information
?
-
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 + alpha,alpha-trehalose[side 1]
[protein]-L-histidine + alpha,alpha-trehalose 6-phosphate[side 2]
show the reaction diagram
enzyme IITre-mediated phosphorylation of trehalose requires the activity of enzyme IIAGlc, a component of the major glucose transport system
-
-
?
[protein]-Npi-phospho-L-histidine + alpha,alpha-trehalose[side 1]
[protein]-L-histidine + alpha,alpha-trehalose 6-phosphate[side 2]
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
trehalose
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enzyme activity is induced by trehalose in the medium but not at high osmolarity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
x * 42000, SDS-PAGE
52308
x * 52308, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boos, W.; Ehmann, U.; Forkl, H.; Klein, W.; Rimmele, M.; Postma, P.
Trehalose transport and metabolism in Escherichia coli
J. Bacteriol.
172
3450-3461
1990
Escherichia coli
Manually annotated by BRENDA team
Klein, W.; Horlacher, R.; Boos, W.
Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose
J. Bacteriol.
177
4043-4052
1995
Escherichia coli (P36672), Escherichia coli
Manually annotated by BRENDA team
Steen, J.A.; Bohlke, N.; Vickers, C.E.; Nielsen, L.K.
The trehalose phosphotransferase system (PTS) in E. coli W can transport low levels of sucrose that are sufficient to facilitate induction of the csc sucrose catabolism operon
PLoS ONE
9
e88688
2014
Escherichia coli, Escherichia coli (A0A0H3F7X9), Escherichia coli DSM 1116 (A0A0H3F7X9)
Manually annotated by BRENDA team