EzCatDB: D00527
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DB codeD00527
RLCP classification3.105.230000.86 : Transfer
CATH domainDomain : Rossmann foldCatalytic domain
Domain 23.40.35.- : Fructose Permease

Enzyme Name

Protein namePTS system mannose-specific EIIAB componentprotein-Npi-phosphohistidine---sugar phosphotransferase

glucose permease

PTS permease

phosphotransferase, phosphohistidinoprotein-hexose

enzyme IIl4ac

gene glC proteins

gene bglC RNA formation factors

PEP-dependent phosphotransferase enzyme II

PEP-sugar phosphotransferase enzyme II

phosphoenolpyruvate-sugar phosphotransferase enzyme II

phosphohistidinoprotein-hexose phosphotransferase

phosphohistidinoprotein-hexose phosphoribosyltransferase

phosphoprotein factor-hexose phosophotransferase

protein, specific or class, gene bglC

ribonucleic acid formation factor, gene glC

sucrose phosphotransferase system II

protein-Npi-phosphohistidine:sugar N-pros-phosphotransferase

protein-Npi-phosphohistidine:sugar Npi-phosphotransferase

IncludesMannose-specific phosphotransferase enzyme IIA component
   EC 2.7.1.-
PTS system mannose-specific EIIA component EIII-Man
Mannose-specific phosphotransferase enzyme IIB component
PTS system mannose-specific EIIB component
RefSeqNP_416331.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_490078.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF03610 (EIIA-man)
PF03830 (PTSIIB_sorb)
[Graphical view]

KEGG pathways
MAP codePathwaysE.C.
MAP00010Glycolysis / Gluconeogenesis2.7.1.69
MAP00051Fructose and mannose metabolism2.7.1.69
MAP00052Galactose metabolism2.7.1.69
MAP00053Ascorbate and aldarate metabolism2.7.1.69
MAP00500Starch and sucrose metabolism2.7.1.69
MAP00530Aminosugars metabolism2.7.1.69

UniProtKB:Accession NumberP69797
ActivityProtein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L- histidine/cysteine.,Protein EIIB N(pi)-phospho-L- histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular locationCytoplasm. Cell inner membrane, Peripheral membrane protein.

Compound table: links to PDB-related databases & PoSSuM

CompoundProtein cysteineProtein N(pi)-phospho-L-histidineSugarProtein S-phosphoryl-cysteineProtein histidineSugar phosphate
Typepeptide/protein,sulfhydryl grouparomatic ring (with nitrogen atoms),peptide/protein,phosphate group/phosphate ionpolysaccharidepeptide/protein,phosphate group/phosphate ion,sulfide grouparomatic ring (with nitrogen atoms),peptide/proteinphosphate group/phosphate ion,polysaccharide



Active-site residues
literature [2]
pdbCatalytic residuesModified residues
1pdoAHIS 10;ASP 67
HIS 10(phosphorylated)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis

PubMed ID8131846
JournalFEBS Lett
AuthorsMarkovic-Housley Z, Balbach J, Stolz B, Genovesio-Taverne JC
TitlePredicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli.
Related UniProtKBP69797
PubMed ID8676384
JournalJ Mol Biol
AuthorsNunn RS, Markovic-Housley Z, Genovesio-Taverne JC, Flukiger K, Rizkallah PJ, Jansonius JN, Schirmer T, Erni B
TitleStructure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution.
Related PDB1pdo
Related UniProtKBP69797
PubMed ID9074635
JournalFEBS Lett
AuthorsGschwind RM, Gemmecker G, Leutner M, Kessler H, Gutknecht R, Lanz R, Flukiger K, Erni B
TitleSecondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures.
Related UniProtKBP69797

The same E.C. number ( appears in S00297, D00525, S00283, S00420. All of them are enzymes in PTS system.
In the phosphotransferase (PTS) system, a phosphoryl group is transferred from phosphoenolpyruvate (PEP) via the PTS enzymes, EI, HPr, IIA, IIB to the tranported sugar.
This enzyme is composed of IIA domain and IIB domain of a mannose transporter (IIAB-mannose).
In the IIA domain, His10 is hydrogen-bonded to a buried Asp67 that is not charge compensated. The carboxylate group of Asp67 acts as a general base and increases the basic strength of the nearby imidazole ring of His10. The nucleophilic attack of the exposed imidazole NE atom onto the phosphorus of phospho-HPr would thus be facilitated.


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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