Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.1.167 - D-glycero-beta-D-manno-heptose-7-phosphate kinase and Organism(s) Escherichia coli and UniProt Accession P76658

for references in articles please use BRENDA:EC2.7.1.167
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The bifunctional protein hldE includes D-glycero-beta-D-manno-heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70). The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. The enzyme selectively produces D-glycero-beta-D-manno-heptose 1,7-bisphosphate .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P76658
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
bifunctional D-beta-D-heptose-7-phosphate kinase/D-beta-dheptose-1-phosphate adenylyltransferase, D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase, D-beta-D-heptose 7-phosphotransferase, D-beta-D-heptose-7-phosphate kinase, glycero-manno-heptose 7-phosphate kinase, heptose 7-phosphate kinase, HldE, HldE1 heptokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase
bifunctional enzyme
D-beta-D-heptose 7-phosphotransferase
-
D-beta-D-heptose-7-phosphate kinase
-
glycero-manno-heptose 7-phosphate kinase
-
heptose 7-phosphate kinase
-
HldE1 heptokinase
-
bifunctional D-beta-D-heptose-7-phosphate kinase/D-beta-dheptose-1-phosphate adenylyltransferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-glycero-beta-D-manno-heptose 7-phosphate 1-phosphotransferase
The bifunctional protein hldE includes D-glycero-beta-D-manno-heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70). The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. The enzyme selectively produces D-glycero-beta-D-manno-heptose 1,7-bisphosphate [5].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
7-O-phosphono-6-deoxy-glycero-D-manno-heptopyranosyl phosphate + ATP
? + ADP
show the reaction diagram
-
low activity
-
-
?
7-phosphate-D-glycero-beta-D-manno-heptose + ATP
D-glycero-D-manno-beta-heptose 1,7-bisphosphate + ADP
show the reaction diagram
-
-
-
-
?
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-mannoheptose 1,7-bisphosphate + ADP
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
synthesis of ADP-D-beta-D-heptose in Escherichia coli requires three proteins, GmhA (sedoheptulose 7-phosphate isomerase), HldE (bifunctional D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase), and GmhB (D,D-heptose 1,7-bisphosphate phosphatase)
-
-
?
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
-
exclusively forming the beta-anomer, namely, D-glycero-beta-D-manno-heptose-1,7-bisphosphate
-
-
?
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-mannoheptose 1,7-bisphosphate + ADP
show the reaction diagram
-
-
-
-
?
additional information
?
-
rfaE encodes a bifunctional protein. It is proposed that domain I is involved in the synthesis of D-glycero-D-manno-heptose 1-phosphate, whereas domain II catalyzes the ADP transfer to form ADP-D-glycero-D-manno-heptose
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional protein hldE includes: D-beta-D-heptose 7-phosphate kinase and D-beta-D-heptose 1-phosphate adenosyltransferase
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83000
gel filtration
55000
-
x * 55000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
HldE comprises two functional domains: an N-terminal region with homology to the ribokinase superfamily (HldE1 domain) and a C-terminal region with homology to the cytidylyltransferase superfamily. HldE functional unit is a dimer and structural components present in each HldE1 monomer are required for enzymatic activity
?
-
x * 55000, SDS-PAGE
additional information
-
the N-terminal domain I spans amino acids 1-318 and shares structural features with members of the ribokinase family. The C-terminal domain II, which spans amino acids 344-477, has all the conserved features of the cytidylyltransferase superfamily
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D264E
loss of activity
D264N
loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure
E198D
loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure
N195D
loss of activity
additional information
-
development of an efficient one-pot three enzymes strategy for chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose (ADP-D, D-heptose) using chemically synthesized D,D-heptose-7-phosphate and the ADP-D,D-heptose biosynthetic enzymes HldE and GmhB, method, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Valvano, M.A.; Marolda, C.L.; Bittner, M.; Glaskin-Clay, M.; Simon, T.L.; Klena, J.D.
The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose
J. Bacteriol.
182
488-497
2000
Escherichia coli (P76658), Salmonella enterica subsp. enterica serovar Typhimurium (Q7CPR9)
Manually annotated by BRENDA team
Kneidinger, B.; Marolda, C.; Graninger, M.; Zamyatina, A.; McArthur, F.; Kosma, P.; Valvano, M.A.; Messner, P.
Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli
J. Bacteriol.
184
363-369
2002
Escherichia coli (P76658)
Manually annotated by BRENDA team
McArthur, F.; Andersson, C.E.; Loutet, S.; Mowbray, S.L.; Valvano, M.A.
Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis
J. Bacteriol.
187
5292-5300
2005
Escherichia coli (P76658), Escherichia coli
Manually annotated by BRENDA team
Valvano, M.A.; Messner, P.; Kosma, P.
Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides
Microbiology
148
1979-1989
2002
Escherichia coli
Manually annotated by BRENDA team
Li, T.; Wen, L.; Williams, A.; Wu, B.; Li, L.; Qu, J.; Meisner, J.; Xiao, Z.; Fang, J.; Wang, P.G.
Chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose and study of the substrate specificity of HldE
Bioorg. Med. Chem.
22
1139-1147
2014
Escherichia coli
Manually annotated by BRENDA team