EzCatDB: S00420
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DB codeS00420
RLCP classification3.105.250000.90 : Transfer
CATH domainDomain 13.40.930.10 : Mannitol-specific EII; Chain ACatalytic domain
E.C.2.7.1.-

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

Enzyme Name
UniProtKB

P69829
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
Activity
Subunit
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC04261C02743C00615L00031
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
ChEBI



PubChem



            
1a6jAUnboundUnboundUnboundUnbound
1a6jBAnalogue:SO4UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot
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
[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 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 (2.7.1.69). 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.

createdupdated
2002-08-302009-02-26


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