DB code: S00420

RLCP classification	3.105.250000.90 : Transfer
CATH domain	3.40.930.10 : Mannitol-specific EII; Chain A	Catalytic domain
E.C.	2.7.1.-
CSA
M-CSA
MACiE

CATH domain	Related DB codes (homologues)
3.40.930.10 : Mannitol-specific EII; Chain A	T00258

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	RefSeq	Pfam
P69829	Nitrogen regulatory protein	EC 2.7.1.- Enzyme IIA-NTR Phosphotransferase enzyme IIA component PTS system EIIA component	NP_417671.1 (Protein) NC_000913.2 (DNA/RNA sequence) YP_491389.1 (Protein) NC_007779.1 (DNA/RNA sequence)	PF00359 (PTS_EIIA_2) [Graphical View]

KEGG enzyme name

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
P69829	PTSN_ECOLI			Cytoplasm.

KEGG Pathways
Map code	Pathways	E.C.

Compound table
	Substrates		Products		Intermediates
KEGG-id	C04261	C02743	C00615	L00031
E.C.
Compound	Protein N(pi)-phospho-L-histidine	Protein cysteine	Protein histidine	Protein S-phosphoryl-cysteine
Type	aromatic ring (with nitrogen atoms),peptide/protein,phosphate group/phosphate ion	peptide/protein,sulfhydryl group	aromatic ring (with nitrogen atoms),peptide/protein	peptide/protein,phosphate group/phosphate ion,sulfide group
ChEBI
PubChem

1a6jA	Unbound	Unbound	Unbound	Unbound
1a6jB	Analogue:SO4	Unbound	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
Swiss-prot

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1a6jA	ARG 57;HIS 73;HIS 120		HIS 73 (phosphorylated)
1a6jB	ARG 57;HIS 73;HIS 120		HIS 73 (phosphorylated)

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[2]	Fig.7, Fig.8, p.385	2
[3]	Fig.3

References
[1]
Resource
Comments
Medline ID
PubMed ID	1946374
Journal	Proc Natl Acad Sci U S A
Year	1991
Volume	88
Pages	9603-7
Authors	Sugiyama JE, Mahmoodian S, Jacobson GR
Title	Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions.
Related PDB
Related UniProtKB	P00550
[2]
Resource
Comments
Medline ID
PubMed ID	9551558
Journal	Structure
Year	1998
Volume	6
Pages	377-88
Authors	van Montfort RL, Pijning T, Kalk KH, Hangyi I, Kouwijzer ML, Robillard GT, Dijkstra BW
Title	The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.
Related PDB	1a3a
Related UniProtKB	P00550
[3]
Resource
Comments
Medline ID
PubMed ID	9636714
Journal	J Mol Biol
Year	1998
Volume	279
Pages	245-55
Authors	Bordo D, van Monfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Dijkstra BW
Title	The three-dimensional structure of the nitrogen regulatory protein IIANtr from Escherichia coli.
Related PDB	1a6j
Related UniProtKB	P69829

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.

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.

Created	Updated
2002-08-30	2009-02-26