EzCatDB: S00297
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DB codeS00297
RLCP classification3.105.250000.48 : Transfer
CATH domainDomain 13.40.50.270 : Rossmann foldCatalytic domain
E.C.2.7.1.69

CATH domainRelated DB codes (homologues)
3.40.50.270 : Rossmann foldS00298

Enzyme Name
UniProtKBKEGG

P69795
Protein nameN,N''-diacetylchitobiose-specific phosphotransferase enzyme IIB 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
SynonymsEC 2.7.1.69
PTS system N,N''-diacetylchitobiose-specific EIIB component
RefSeqNP_416252.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489999.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF02302 (PTS_IIB)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00051Fructose and mannose metabolism
MAP00052Galactose metabolism
MAP00053Ascorbate and aldarate metabolism
MAP00500Starch and sucrose metabolism
MAP00530Aminosugars metabolism

UniProtKB:Accession NumberP69795
Entry namePTQB_ECOLI
ActivityProtein EIIB N(pi)-phospho-L- histidine/cysteine + sugar = protein EIIB + sugar phosphate.
SubunitMonomer, in both its unphosphorylated and phosphorylated forms.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC04261C11477C00615C00934
CompoundProtein N(pi)-phospho-L-histidineSugarProtein histidineSugar phosphate
Typearomatic ring (with nitrogen atoms),peptide/protein,phosphate group/phosphate ionpolysaccharidearomatic ring (with nitrogen atoms),peptide/proteinphosphate group/phosphate ion,polysaccharide
ChEBI



PubChem



            
1e2bAUnboundUnboundUnboundUnbound
1iibAUnboundUnboundUnboundUnbound
1iibBUnboundUnboundUnboundUnbound
1h9cAUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot,Phosphorylation site
pdbCatalytic residuesModified residuescomment
           
1e2bA      
 
mutant C10S
1iibA      
 
mutant C10S
1iibB      
 
mutant C10S
1h9cACSP 10
CSP 10 (phosphorylated cys)
phosphorylation site

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.221-222

references
[1]
PubMed ID2092358
JournalRes Microbiol
Year1990
Volume141
Pages1061-7
AuthorsReizer J, Reizer A, Saier MH Jr
TitleThe cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus.
Related UniProtKBP69795
[2]
PubMed ID8003964
JournalProtein Sci
Year1994
Volume3
Pages282-90
AuthorsAb E, Schuurman-Wolters GK, Saier MH, Reizer J, Jacuinod M, Roepstorff P, Dijkstra K, Scheek RM, Robillard GT
TitleEnzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy.
Related UniProtKBP69795
[3]
PubMed ID9041631
JournalProtein Sci
Year1997
Volume6
Pages304-14
AuthorsAb E, Schuurman-Wolters G, Reizer J, Saier MH, Dijkstra K, Scheek RM, Robillard GT
TitleThe NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
Related PDB1e2b
Related UniProtKBP69795
[4]
PubMed ID9032081
JournalStructure
Year1997
Volume5
Pages217-25
Authorsvan Montfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Thunnissen MM, Robillard GT, Dijkstra BW
TitleThe structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.
Related PDB1iib
Related UniProtKBP69795

comments
The same E.C. number (2.7.1.69) appears in D00527, D00525, S00283, S00420, 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 IIB subunit of a cellobiose transporter (IIB-cellobiose).
The transfer of the phosphoryl group proceeds via an associative mechanism with a pentavalent phosphorus intermediate. Although positively charged residues are usually important for the stabilization of the negatively charged reaction intermediate, IIB-cellobiose lacks not only such residues but also any other positively charged residues. This suggests that in the phosphotransfer reactions between IIA-cellobiose and IIB-cellobiose, and between IIB-cellobiose and the translocated cellobiose, stabilization of the respective transition states is carried out by residues located on IIA-cellobiose and the membrane-bound IIC-cellobiose, respectively.

createdupdated
2002-07-272009-03-04


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