Information on EC 2.7.4.30 - lipid A phosphoethanolamine transferase

Word Map on EC 2.7.4.30
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.4.30
-
RECOMMENDED NAME
GeneOntology No.
lipid A phosphoethanolamine transferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
diacylphosphatidylethanolamine + lipid A 1-(2-aminoethyl diphosphate) = diacylglycerol + lipid A 1,4'-bis(2-aminoethyl diphosphate)
show the reaction diagram
(3)
-
-
-
diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
(1)
-
-
-
diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
(2)
-
-
-
SYSTEMATIC NAME
IUBMB Comments
diacylphosphatidylethanolamine:lipid-A phosphoethanolaminetransferase
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
diverse colistin sensitive and resistant strains, gene pmrA
UniProt
Manually annotated by BRENDA team
gene cj0256 or eptC
UniProt
Manually annotated by BRENDA team
gene lptA
-
-
Manually annotated by BRENDA team
gene Hp0022 or eptA
UniProt
Manually annotated by BRENDA team
gene Hp0022 or eptA
UniProt
Manually annotated by BRENDA team
gene lptA
UniProt
Manually annotated by BRENDA team
gene lptA
-
-
Manually annotated by BRENDA team
gene lptA
UniProt
Manually annotated by BRENDA team
serovar Typhimurium, gene pmrA
UniProt
Manually annotated by BRENDA team
serovar typhimurium, gene eptA or pmrC
UniProt
Manually annotated by BRENDA team
a lpxM mutant strain, gene pmrA
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
ethanolamine transferases are members of the YhjW/YjdB/YijP superfamily
malfunction
metabolism
physiological function
additional information
analysis of the three-dimensional structure of the soluble catalytic domain of LptA, active-site residues, structure homology, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dihexanoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
low activity, addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dihexanoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
low activity, addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
Q7DD94
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
Q7DD94
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
?
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
required, the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+
Mg2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases
Zn2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases, interaction of the Zn2+ with the active site, binding site structure, overview. The second Zn2+ ion is coordinated by the side chains of His383, His465, and one of the oxygen atoms of the phosphate group attached to Thr280. In LptA, two types of coordination around the Zn1 are observed depending on the state of Thr280. In the case of non-phosphorylated Thr280, the coordination about Zn1 is tetrahedral with the fourth ligand being the free phosphate group. In contrast, when Thr280 is phosphorylated, a penta-coordinated metal is observed with the hydroxyl oxygen atom of Thr280 and one of the phosphate oxygen atoms each interacting weakly with the metal
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PmrA
te enzyme EptA is activated in a PmrA-dependent manner, overview
-
additional information
the PmrA-activated pmrC gene encodes an inner membrane protein that is required for the incorporation of phosphoethanolamine into lipid A and for polymyxin B resistance, mutational analysis, overview
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
colistin resistant strains show higher enzyme expression compared to colistin sensitive strains, enzyme expression analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation of the putative nucleophile, Thr280
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged soluble catalytic domain of LptA, free and selenomethionine-labeled, or in complex with Zn2+ and a truncated form of substrate 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine, X-ray diffraction structure determination and analysis at 1.43-1.78 A resolution, molecular replacement. and modeling
recombinant His-tagged membrane-deletion mutant enzyme, mixing of 0.001 ml of 5.2 mg/ml protein in 50 mM HEPES, pH 8.0, 50 mM sodium chloride, with 0.001 ml of crystallization solution containing 23-26% PEG 8000, 100 mM ammonium sulfate, 100 mM HEPES, pH 7.5–8.0, 15 mM n-dodecyl-N,N-dimethylamine-N-oxide, and 200 nl of microseeding solution, 20°C, 3-5 days, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged membrane-deletion mutant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis
recombinant wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene cj0256 or eptC
-
gene cj0256, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli K-12 strain W3110/EC01
gene Hp0022, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli NovaBlue(DE3) membranes. method optimization
gene lptA
gene lptA, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli
-
gene lptA, expression from a a multicopy plasmid in Neisseria meningitidis, construction of an lptA-FLAG epitope-tagged fusion Neisseria meningitidis strain HT1295 from strain H44/76
gene pmrA, genetic organization of the pmrCAB genes, PCR-based expression analysis in colistin sensitive and resistant strains
gene pmrA, sequence comparisons with Neisseria meningitidis phosphoethanolamine phosphotransferases lptA, lpt3, and lpt6; gene pmrC
recombinant expression of His-tagged membrane-deletion mutant enzyme in Escherichia coli strain BL21(DE3)pLysS
recombinant expression of wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme in Escherichia coli strains CKEC272 and CKEC580
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of EptA (PmrC) is under the control of PmrA/PmrB
no upregulation of pmrA by Fe3+ and Mg2+ in strain ATCC 19606
the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+, induction is lost in enzyme mutant strain CH020 (DELTApmrA)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information