Information on EC 2.7.8.30 - undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

for references in articles please use BRENDA:EC2.7.8.30
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:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.8.30
deleted. Now EC 2.4.2.53
RECOMMENDED NAME
GeneOntology No.
undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
cf. 3.1.3.27
UniProt
Manually annotated by BRENDA team
cf. 3.1.3.27
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl phosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
show the reaction diagram
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A-(2-aminoethyl diphosphate)
show the reaction diagram
-
-
LptA decorates one position of the Escherichia coli lipid A headgroups with phosphatidylethanolamine
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of the soluble domain of the lipid A phosphoethanolamine transferase, to 1.4 A resolution. The structure reveals a core hydrolase fold similar to that of alkaline phosphatase. Loop regions in the structure differ, presumably to enable interaction with the membrane-localized substrates and to provide substrate specificity. A phosphorylated form of the putative nucleophile, Thr280, is observed. Metal ions in the active site are coordinated to Thr280 and to residues conserved among the family of transferases
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of EptA is regulated by zinc via the ColRS two-component system. ColR specifically induces phosphoethanolamine addition to lipid A in lieu of L-Ara4N when Zn2+ is present