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
E.C.2.7.1.69,2.7.1.-

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

Enzyme Name
UniProtKBKEGG

P00550
Protein namePTS system mannitol-specific EIICBA componentprotein-Npi-phosphohistidine---sugar phosphotransferase
   (EC 2.7.1.69)

glucose permease
   (EC 2.7.1.69)

PTS permease
   (EC 2.7.1.69)

phosphotransferase, phosphohistidinoprotein-hexose
   (EC 2.7.1.69)

enzyme IIl4ac
   (EC 2.7.1.69)

gene glC proteins
   (EC 2.7.1.69)

gene bglC RNA formation factors
   (EC 2.7.1.69)

PEP-dependent phosphotransferase enzyme II
   (EC 2.7.1.69)

PEP-sugar phosphotransferase enzyme II
   (EC 2.7.1.69)

phosphoenolpyruvate-sugar phosphotransferase enzyme II
   (EC 2.7.1.69)

phosphohistidinoprotein-hexose phosphotransferase
   (EC 2.7.1.69)

phosphohistidinoprotein-hexose phosphoribosyltransferase
   (EC 2.7.1.69)

phosphoprotein factor-hexose phosophotransferase
   (EC 2.7.1.69)

protein, specific or class, gene bglC
   (EC 2.7.1.69)

ribonucleic acid formation factor, gene glC
   (EC 2.7.1.69)

sucrose phosphotransferase system II
   (EC 2.7.1.69)

protein-Npi-phosphohistidine:sugar N-pros-phosphotransferase
   (EC 2.7.1.69)

protein-Npi-phosphohistidine:sugar Npi-phosphotransferase
   (EC 2.7.1.69)

SynonymsEIICBA-Mtl
EII-Mtl
IncludesMannitol permease IIC component PTS system mannitol-specific EIIC component
Mannitol-specific phosphotransferase enzyme IIB component
   EC 2.7.1.69
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.
SubunitHomodimer.
Subcellular locationCell inner membrane, Multi-pass membrane protein.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC04261C11477C02743C00615C00934L00031
E.C.2.7.1.69,2.7.1.-2.7.1.692.7.1.-2.7.1.69,2.7.1.-2.7.1.692.7.1.-
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
ChEBI





PubChem





              
1a3aAUnboundUnboundUnboundUnboundUnboundUnbound
1a3aBUnboundUnboundUnboundUnboundUnboundUnbound
1a3aCUnboundUnboundUnboundUnboundUnboundUnbound
1a3aDUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot
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
[3]Fig.3

references
[1]
PubMed ID1946374
JournalProc Natl Acad Sci U S A
Year1991
Volume88
Pages9603-7
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
[2]
PubMed ID9551558
JournalStructure
Year1998
Volume6
Pages377-88
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
[3]
PubMed ID9636714
JournalJ Mol Biol
Year1998
Volume279
Pages245-55
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

comments
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. 2.7.1.69), and the C-terminal domain for Mannitol-specific phosphotransferase enzyme IIA component (E.C. 2.7.1.-).
The same E.C. number (2.7.1.69) 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.

createdupdated
2002-08-302009-03-04


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