Information on EC 6.3.1.14 - diphthine-ammonia ligase

for references in articles please use BRENDA:EC6.3.1.14
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
Include results (AMENDA + additional results, but less precise)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.1.14
-
RECOMMENDED NAME
GeneOntology No.
diphthine-ammonia ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + diphthine-[translation elongation factor 2] + NH3 = AMP + diphosphate + diphthamide-[translation elongation factor 2]
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptide synthase reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
diphthamide biosynthesis I (archaea)
-
-
diphthamide biosynthesis II (eukaryotes)
-
-
SYSTEMATIC NAME
IUBMB Comments
diphthine-[translation elongation factor 2]:ammonia ligase (AMP-forming)
This amidase catalyses the last step in the conversion of an L-histidine residue in the translation elongation factor EF2 to diphthamide. This factor is found in all archaebacteria and eukaryotes, but not in eubacteria, and is the target of bacterial toxins such as the diphtheria toxin and the Pseudomonas exotoxin A (see EC 2.4.2.36, NAD+---diphthamide ADP-ribosyltransferase). The substrate of the enzyme, diphthine, is produced by EC 2.1.1.98, diphthine synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
114514-33-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CHO-K1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae ATCC 204508 / S288c
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
Dph7, i.e. YBR246w, apparently couples diphthine synthase to diphthine amidation. Dph6 and Dph7 are components required for the amidation step of the diphthamide pathway. In contrast to Dph6, Dph7 may be regulatory. DPH6 and DPH7 are novel sordarin effectors, a feature they share with the diphthamide synthesis genes DPH1-DPH5
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + diphthine + ammonia
ADP + phosphate + diphthamide
show the reaction diagram
ATP + diphthine-[peptide 686-VNILDVTLHADAIHR-700] + NH3
AMP + diphosphate + diphthamide-[peptide 686-VNILDVTLHADAIHR-700]
show the reaction diagram
eEF2-derived peptide sequence
-
-
?
ATP + diphthine-[translation elongation factor 2] + NH3
AMP + diphosphate + diphthamide-[translation elongation factor 2]
show the reaction diagram
CTP + diphthine + ammonia
CDP + phosphate + diphthamide
show the reaction diagram
GTP + diphthine + ammonia
GDP + phosphate + diphthamide
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
ATP + diphthine-[translation elongation factor 2] + NH3
AMP + diphosphate + diphthamide-[translation elongation factor 2]
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene DPH6, the gene is identified through mining the DPH1-DPH5 interaction network
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (122 entries)
Please use the Sequence Search for a specific query.