EzCatDB: T00258
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DB codeT00258
RLCP classification3.105.250000.90 : Transfer
CATH domainDomain 1-.-.-.-
Domain 23.40.50.- : Rossmann fold
Domain 33.40.930.10 : Mannitol-specific EII; Chain ACatalytic domain

CATH domainRelated DB codes (homologues)
3.40.930.10 : Mannitol-specific EII; Chain AS00420

Enzyme Name

Protein namePTS system mannitol-specific EIICBA 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

IncludesMannitol permease IIC component PTS system mannitol-specific EIIC component
Mannitol-specific phosphotransferase enzyme IIB component
PTS system mannitol-specific EIIB component
Mannitol-specific phosphotransferase enzyme IIA component
   EC 2.7.1.-
PTS system mannitol-specific EIIA component
RefSeqNP_418056.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491835.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF00359 (PTS_EIIA_2)
PF02378 (PTS_EIIC)
PF02302 (PTS_IIB)
[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 NumberP00550
Entry namePTM3C_ECOLI
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 locationCell inner membrane, Multi-pass membrane protein.

Compound table: links to PDB-related databases & PoSSuM

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



Active-site residues
pdbCatalytic residuesModified residues
1a3aAARG 49;HIS 65;HIS 111
HIS 65 (phosphorylated)
1a3aBARG 49;HIS 65;HIS 111
HIS 65 (phosphorylated)
1a3aCARG 49;HIS 65;HIS 111
HIS 65 (phosphorylated)
1a3aDARG 49;HIS 65;HIS 111
HIS 65 (phosphorylated)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.7, Fig.8, p.3852

PubMed ID1946374
JournalProc Natl Acad Sci U S A
AuthorsSugiyama JE, Mahmoodian S, Jacobson GR
TitleMembrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions.
Related UniProtKBP00550
PubMed ID9551558
Authorsvan Montfort RL, Pijning T, Kalk KH, Hangyi I, Kouwijzer ML, Robillard GT, Dijkstra BW
TitleThe structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.
Related PDB1a3a
Related UniProtKBP00550
PubMed ID9636714
JournalJ Mol Biol
AuthorsBordo D, van Monfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Dijkstra BW
TitleThe three-dimensional structure of the nitrogen regulatory protein IIANtr from Escherichia coli.
Related PDB1a6j
Related UniProtKBP69829

This enzyme is composed of three domains: The N-terminal domain for Mannitol permease IIC component, a domain for Mannitol-specific phosphotransferase enzyme IIB component (E.C., and the C-terminal domain for Mannitol-specific phosphotransferase enzyme IIA component (E.C. 2.7.1.-).
The same E.C. number ( appears in S00297, D00527, S00283, S00046. 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. The enzyme here is IIA subunit of a mannitol transporter (IIA-mannitol).
His65 (1a3a) is phosphorylated during the phosphotransfer reaction. A phosphoryl transfer between two PTS proteins involves an in-line attack of the phosphorus atom by the acceptor protein. A trigonal bipyramidal transition state is formed with a pentavalent coordination of the phosphorus atom. Productive breakdown of the transition state results in an inversion of the configuration at the phosphorus atom [2]. Although there is no biochemical evidence for the roles of Arg49/His111 (1a3a), Arg49 is ideally positioned to stabilize the transition state in the phosphoryl transfer from HPr to IIA-mannitol. In contrast, whilst His111 is pointed away from the phosphorylation site for HPr, it might also be needed for the phosphoryl transfer to IIB-mannitol.


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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