Information on EC 3.1.3.79 - mannosylfructose-phosphate phosphatase

for references in articles please use BRENDA:EC3.1.3.79
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The expected taxonomic range for this enzyme is: Agrobacterium tumefaciens

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EC NUMBER
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3.1.3.79
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RECOMMENDED NAME
GeneOntology No.
mannosylfructose-phosphate phosphatase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
beta-D-fructofuranosyl-alpha-D-mannopyranoside 6F-phosphate + H2O = beta-D-fructofuranosyl-alpha-D-mannopyranoside + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mannosylfructose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
beta-D-fructofuranosyl-alpha-D-mannopyranoside-6F-phosphate phosphohydrolase
This enzyme, from the soil proteobacterium and plant pathogen Agrobacterium tumefaciens strain C58, requires Mg2+ for activity. Mannosylfructose is the major endogenous osmolyte produced by several alpha-proteobacteria in response to osmotic stress and is synthesized by the sequential action of EC 2.4.1.246 (mannosylfructose-phosphate synthase) followed by this enzyme. While mannosylfructose 6-phosphate is the physiological substrate, the enzyme can use sucrose 6-phosphate very efficiently. The F in mannosylfructose 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
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ORGANISM
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LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Agrobacterium tumefaciens C58 / ATCC 33970
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Uniprot
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
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LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-fructofuranosyl-alpha-D-mannopyranoside 6F-phosphate + H2O
beta-D-fructofuranosyl-alpha-D-mannopyranoside + phosphate
show the reaction diagram
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LINKS TO OTHER DATABASES (specific for EC-Number 3.1.3.79)
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)