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Information on EC 3.1.3.46 - fructose-2,6-bisphosphate 2-phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9MB58
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3.1.3.46 fructose-2,6-bisphosphate 2-phosphataseIUBMB Comments
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
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Word Map
- 3.1.3.46
- fructose-1,6-bisphosphatase
-
gluconeogenesis
-
gluconeogenic
- amp
- 6-phosphate
-
1,6-bisphosphatase
-
tp53-induced
- phosphoenolpyruvate
- isozyme
- chloroplast
- endothelial
- glycogen
- pentose
- 6-phosphofructo-1-kinase
- hepatocytes
-
carboxykinase
- fructose-6-phosphate
-
hypoxia-inducible
- glucokinase
-
camp-dependent
-
warburg
- pepck
-
3.1.3.11
-
glucose-induced
- g6pase
- spinach
- hk2
-
fructose-1
- hypoglycemia
- glucose-6-phosphatase
- hexokinase
-
fru-6-p
-
glycogenolysis
-
calvin
-
p53-inducible
-
anaphase-promoting
- phosphofructokinase-1
- phosphoenzyme
-
fructose-6-p
- molecular biology
- medicine
- pharmacology
- agriculture
-
pentose-phosphate
-
z-line
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
fbpase, pfkfb3, tigar, pfk-2, pfkfb4, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, fructose-2,6-bisphosphatase, pfkfb2, pfk-2/fbpase-2, f-2,6-p2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-fructose-2,6-bisphosphatase
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-
-
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fructose-2,6-bisphosphatase
-
-
-
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fructose-2,6-diphosphatase
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-
-
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phosphatase, fructose 2,6-di-
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
beta-D-fructose-2,6-bisphosphate 2-phosphohydrolase
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
CAS REGISTRY NUMBER
COMMENTARY
81611-75-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
SwissProt
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme, expressed in yeast
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). F26_ARATH
744
0
82559
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
92000
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
96000
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphorylatiopn of serine and threonine residues, phosphorylation status is regulated physiologically and developmentally
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
N-terminal truncation mutants, behave as monomers, show a decrease in the kinase/phosphatase ration by 4-fold, role of N-terminus for subunit assembly and kinetic properties
additional information
-
N-terminal truncation mutants, behave as monomers, show a decrease in the kinase/phosphatase ration by 4-fold, role of N-terminus for subunit assembly and kinetic properties
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Arabidopsis using the Agrobacterium tumefaciens GV3101 mediated floral dip method, gene knockout mutants and RNAi mutants, overexpression induces increased levels of soluble sugars, declined starch and triose phosphate content, beta-D-fructose 2,6-bisphosphate contributes to the regulation of starch and sucrose levels
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Villadsen, D.; Nielsen, T.H.
N-terminal truncation affects the kinetics and structure of fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana
Biochem. J.
359
591-597
2001
Arabidopsis thaliana (Q9MB58), Arabidopsis thaliana
Furumoto, T.; Teramoto, M.; Inada, N.; Ito, M.; Nishida, I.; Watanabe, A.
Phosphorylation of a bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase, is regulated physiologically and developmentally in rosette leaves of Arabidopsis thaliana
Plant Cell Physiol.
42
1044-1048
2001
Arabidopsis thaliana (Q9MB58), Arabidopsis thaliana
Rider, M.H.; Bertrand, L.; Vertommen, D.; Michels, P.A.; Rousseau, G.G.; Hue, L.
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis
Biochem. J.
381
561-579
2004
Arabidopsis thaliana (Q9MB58), Bos taurus (P26285), Bos taurus (P49872), Bos taurus (Q28901), Desulfovibrio desulfuricans, Drosophila melanogaster (Q9VWH7), Homo sapiens (O60825), Homo sapiens (P16118), Homo sapiens (Q16875), Homo sapiens (Q16877), Leishmania major, Mus musculus (P70265), Mus musculus (Q9ESY2), Rattus norvegicus (O35552), Rattus norvegicus (P07953), Rattus norvegicus (P25114), Rattus norvegicus (Q9JJH5), Schizosaccharomyces pombe
Lee, Y.H.; Lee, D.S.; Lim, J.M.; Yoon, J.M.; Bhoo, S.H.; Jeon, J.S.; Hahn, T.R.
Carbon-partitioning in Arabidopsis is regulated by the fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase enzyme
J. Plant Biol.
49
70-79
2006
Arabidopsis thaliana
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