EzCatDB: S00420
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00420
RLCP classification3.105.250000.90 : Transfer
CATH domainDomain 13.40.930.10 : Mannitol-specific EII; Chain ACatalytic domain

CATH domainRelated DB codes (homologues)
3.40.930.10 : Mannitol-specific EII; Chain AT00258

Enzyme Name

Protein nameNitrogen regulatory protein
SynonymsEC 2.7.1.-
Enzyme IIA-NTR
Phosphotransferase enzyme IIA component
PTS system EIIA component
RefSeqNP_417671.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491389.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF00359 (PTS_EIIA_2)
[Graphical view]

UniProtKB:Accession NumberP69829
Entry namePTSN_ECOLI
Subcellular locationCytoplasm.

Compound table: links to PDB-related databases & PoSSuM

CompoundProtein N(pi)-phospho-L-histidineProtein cysteineProtein histidineProtein S-phosphoryl-cysteine
Typearomatic ring (with nitrogen atoms),peptide/protein,phosphate group/phosphate ionpeptide/protein,sulfhydryl grouparomatic ring (with nitrogen atoms),peptide/proteinpeptide/protein,phosphate group/phosphate ion,sulfide group



Active-site residues
pdbCatalytic residuesModified residues
1a6jAARG 57;HIS 73;HIS 120
HIS 73 (phosphorylated)
1a6jBARG 57;HIS 73;HIS 120
HIS 73 (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 involved in PTS system, to which the other phosphoryl transferases (S00297, D00527, D00525, S00283, S00420 in EzCatDB) also belong. Many of such enzymes have got the same E.C. number ( This enzyme also had the same E.C. number previously, which was changed to 2.7.1.-.
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).
His73 (PDB;1a6J) 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 Arg57/His120 (1a3a), Arg57 is ideally positioned to stabilize the transition state in the phosphoryl transfer from HPr to IIA-mannitol. In contrast, whilst His120 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 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.