Information on EC 3.6.1.63 - alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

for references in articles please use BRENDA:EC3.6.1.63
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 expected taxonomic range for this enzyme is: Escherichia coli

top print hide
EC NUMBER
COMMENTARY hide
3.6.1.63
-
top print hide
RECOMMENDED NAME
GeneOntology No.
alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
show the reaction diagram
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(aminomethyl)phosphonate degradation
-
-
glyphosate degradation III
-
-
methylphosphonate degradation I
-
-
methylphosphonate degradation II
-
-
Phosphonate and phosphinate metabolism
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
alpha-D-ribose-1-methylphosphonate-5-triphosphate diphosphohydrolase
Isolated from the bacterium Escherichia coli.
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
in vivo complementation of the strains, in which phnC to phnP or phnH to phnP are deleted, with plasmids carrying various fragments of the phn operon reveal that the expression of phnC-phnP gene products is essential to restore growth on minimal medium with phosphonate as the sole phosphorus source, while phnG-phnM gene products are required for carbon-phosphorus lyase activity. The minimum size of the DNA required for the whole-cell carbon-phosphorus lyase activity is determined to be a 5.8-kb fragment, encompassing the phnG to phnM genes
physiological function
-
nine gene products (PhnG, PhnH, PhnI, PhnJ, PhnK, PhnL, PhnM, PhnN, and PhnP) comprise a membrane-associated carbon-phosphorus lyase enzyme complex
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O
alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-diphosphate + H2O
D-ribose 5-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-triphosphate + H2O
D-ribose 5-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
110
alpha-D-ribose 1-methylphosphonate 5-triphosphate
-
pH 8.5, temperature not specified in the publication
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
assay at
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
membrane protein
Manually annotated by BRENDA team
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41700
-
SDS-PAGE
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified using gel filtration with a High Load Superdex 200 26/60 prep grade column followed by anion exchange chromatography
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the pSPORT1 vector and expressed in Escherichia coli
-
expressed in Escherichia coli
-
top
Show AA Sequence (208 entries)
Please use the Sequence Search for a specific query.
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 3.6.1.63)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)