Information on EC 3.1.3.73 - adenosylcobalamin/alpha-ribazole phosphatase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
3.1.3.73
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RECOMMENDED NAME
GeneOntology No.
adenosylcobalamin/alpha-ribazole phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenosylcobalamin 5'-phosphate + H2O = coenzyme B12 + phosphate
show the reaction diagram
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-
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alpha-ribazole 5'-phosphate + H2O = alpha-ribazole + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-methyladeninyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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4-methylphenyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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5-hydroxybenzimidazolyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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5-methoxy-6-methylbenzimidazolyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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5-methoxybenzimidazolyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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5-methylbenzimidazolyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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adeninyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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adenosylcobalamin biosynthesis from adenosylcobinamide-GDP I
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adenosylcobalamin biosynthesis from adenosylcobinamide-GDP II
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benzimidazolyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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phenyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP
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superpathway of adenosylcobalamin salvage from cobinamide I
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superpathway of adenosylcobalamin salvage from cobinamide II
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vitamin B12 metabolism
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Porphyrin and chlorophyll metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
adenosylcobalamin/alpha-ribazole-5?-phosphate phosphohydrolase
This enzyme catalyses the last step in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, characterized in Salmonella enterica [3]. It also participates in a salvage pathway that recycles cobinamide into adenosylcobalamin [1].
CAS REGISTRY NUMBER
COMMENTARY hide
251991-06-7
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the effect of the lack of CobC enzyme on AdoCbl synthesis is most evident when the demand for AdoCbl is high, e.g., during growth on ethanolamine as carbon and energy source. However, when the demand for AdoCbl is low (e.g., synthesis of methionine via the Cbl-dependent methionine synthase), there is no detectable effect on Cbl-dependent growth unless the strain also harbors a null allele of the cobT gene encoding the NaMN:DMB phosphoribosyltransferase enzyme. It is possible that under conditions where low levels of AdoCbl are sufficient to support growth, the activity of a non-specific phosphatase generates alpha-ribazole bypassing the need for CobC activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosylcobalamin 5'-phosphate + H2O
adenosylcobalamin + phosphate
show the reaction diagram
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-
-
?
alpha-ribazole 5'-phosphate + H2O
alpha-ribazole + phosphate
show the reaction diagram
alpha-ribazole-5'-phosphate + H2O
alpha -ribazole + phosphate
show the reaction diagram
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-
-
-
?
N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole + H2O
N1-alpha-D-ribosyl-5,6-dimethylbenzimidazole + phosphate
show the reaction diagram
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-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
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
alpha-ribazole 5'-phosphate + H2O
alpha-ribazole + phosphate
show the reaction diagram
alpha-ribazole-5'-phosphate + H2O
alpha -ribazole + phosphate
show the reaction diagram
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.07
alpha-ribazole 5'-phosphate
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5.5 - 13.6
p-nitrophenol phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
substrate p-nitrophenyl phosphate
PDB
SCOP
CATH
UNIPROT
ORGANISM
P52086
Escherichia coli (strain K12);
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-terminal domain (RNase activity), sitting drop method
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose affinity chromatography, gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cobC gene mapped, cloned, sequenced and overexpressed
computer analysis of the cobC and cobD sequences predicts the regulatory regions of these genes to be embedded in the neighbor's coding sequence with only one base pair separating the cobD and cobC coding sequences, the cobC gene is divergently transcribed from the cobD gene
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maltose binding protein fusion protein expressed in Escherichia coli
Mm2058 protein is expressed with a decahistidine tag at its N-terminus
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