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Information on EC 4.7.1.1 - alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase and Organism(s) Escherichia coli and UniProt Accession P16688

for references in articles please use BRENDA:EC4.7.1.1
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IUBMB Comments
This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. Contains an [4Fe-4S] cluster. The enzyme from the bacterium Escherichia coli can act on additional alpha-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. alpha-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and alpha-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).
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This record set is specific for:
Escherichia coli
UNIPROT: P16688
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
P279_10500, phnJ, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
alpha-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane forming)
This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. Contains an [4Fe-4S] cluster. The enzyme from the bacterium Escherichia coli can act on additional alpha-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. alpha-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and alpha-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).
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-phosphate
alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate + methane
show the reaction diagram
alpha-D-ribose 1-methylphosphonate 5-phosphate
alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate + methane
show the reaction diagram
-
-
-
-
?
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
alpha-D-ribose 1-methylphosphonate 5-phosphate
alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate + methane
show the reaction diagram
-
-
-
?
alpha-D-ribose 1-methylphosphonate 5-phosphate
alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate + methane
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
enzyme binds 2.2 equivalents of iron per monomer
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
deletion of the enzyme gene from Escherichia coli leads to the detection of alpha-D-ribose 1-methylphosphonate in the growth medium. alpha-D-Ribose 1-methylphosphonate is the ultimate substrate for the actual C-P lyase reaction
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31800
-
x * 31800, calculated from amino acid sequence
38000
-
x * 38000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C241A
inactive
C244A
inactive
C266A
inactive
C272A
inactive
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kamat, S.S.; Williams, H.J.; Raushel, F.M.
Intermediates in the transformation of phosphonates to phosphate by bacteria
Nature
480
570-573
2011
Escherichia coli, Escherichia coli (P16688)
Manually annotated by BRENDA team
Hove-Jensen, B.; McSorley, F.R.; Zechel, D.L.
Physiological role of phnP-specified phosphoribosyl cyclic phosphodiesterase in catabolism of organophosphonic acids by the carbon-phosphorus lyase pathway
J. Am. Chem. Soc.
133
3617-3624
2011
Escherichia coli, Escherichia coli HO2536
Manually annotated by BRENDA team
Kamat, S.S.; Williams, H.J.; Dangott, L.J.; Chakrabarti, M.; Raushel, F.M.
The catalytic mechanism for aerobic formation of methane by bacteria
Nature
497
132-136
2013
Escherichia coli (P16688)
Manually annotated by BRENDA team
Jochimsen, B.; Lolle, S.; McSorley, F.R.; Nabi, M.; Stougaard, J.; Zechel, D.L.; Hove-Jensen, B.
Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway
Proc. Natl. Acad. Sci. USA
108
11393-11398
2011
Escherichia coli, Escherichia coli HO2735
Manually annotated by BRENDA team