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This is the Wikipedia entry entitled "Fructose 1,6-bisphosphatase". More...
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Fructose 1,6-bisphosphatase Edit Wikipedia article
Fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex. Rendered from PDB 3FBP.
|Locus||Chr. 9 q22.3|
crystal structure of rabbit liver fructose-1,6-bisphosphatase at 2.3 angstrom resolution
crystal structure of fructose-1,6-bisphosphatase
Fructose bisphosphatase (EC 184.108.40.206) is an enzyme that converts fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis and the Calvin cycle which are both anabolic pathways. Fructose bisphosphatase catalyses the reverse of the reaction which is catalysed by phosphofructokinase in glycolysis. These enzymes only catalyse the reaction in one direction each, and are regulated by metabolites such as fructose 2,6-bisphosphate so that high activity of one of the two enzymes is accompanied by low activity of the other. More specifically, fructose 2,6-bisphosphate allosterically inhibits fructose 1,6-bisphosphatase, but activates phosphofructokinase-I. Fructose 1,6-bisphosphatase is involved in many different metabolic pathways and found in most organisms. FBPase requires metal ions for catalysis (Mg2+ and Mn2+ being preferred) and the enzyme is potently inhibited by Li+.
The fold of fructose-1,6-bisphosphatase from pig was noted to be identical to that of inositol-1-phosphatase (IMPase). Inositol polyphosphate 1-phosphatase (IPPase), IMPase and FBPase share a sequence motif (Asp-Pro-Ile/Leu-Asp-Gly/Ser-Thr/Ser) which has been shown to bind metal ions and participate in catalysis. This motif is also found in the distantly-related fungal, bacterial and yeast IMPase homologues. It has been suggested that these proteins define an ancient structurally conserved family involved in diverse metabolic pathways, including inositol signalling, gluconeogenesis, sulphate assimilation and possibly quinone metabolism.
Three different groups of FBPases have been identified in eukaryotes and bacteria (FBPase I-III). None of these groups have been found in archaea so far, though a new group of FBPases (FBPase IV) which also show inositol monophosphatase activity has recently been identified in archaea.
A new group of FBPases (FBPase V) is found in thermophilic archaea and the hyperthermophilic bacterium Aquifex aeolicus. The characterised members of this group show strict substrate specificity for FBP and are suggested to be the true FBPase in these organisms. A structural study suggests that FBPase V has a novel fold for a sugar phosphatase, forming a four-layer alpha-beta-beta-alpha sandwich, unlike the more usual five-layered alpha-beta-alpha-beta-alpha arrangement. The arrangement of the catalytic side chains and metal ligands was found to be consistent with the three-metal ion assisted catalysis mechanism proposed for other FBPases.
The fructose 1,6-bisphosphatases found within the Firmicutes (low GC Gram-positive bacteria) do not show any significant sequence similarity to the enzymes from other organisms. The Bacillus subtilis enzyme is inhibited by AMP, though this can be overcome by phosphoenolpyruvate, and is dependent on Mn(2+). Mutants lacking this enzyme are apparently still able to grow on gluconeogenic growth substrates such as malate and glycerol.
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
- The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".
- Marcus F, Harrsch PB (May 1990). "Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase". Arch. Biochem. Biophys. 279 (1): 151–7. doi:10.1016/0003-9861(90)90475-E. PMID 2159755.
- Marcus F, Gontero B, Harrsch PB, Rittenhouse J (March 1986). "Amino acid sequence homology among fructose-1,6-bisphosphatases". Biochem. Biophys. Res. Commun. 135 (2): 374–81. doi:10.1016/0006-291X(86)90005-7. PMID 3008716.
- Zhang Y, Liang JY, Lipscomb WN (February 1993). "Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase". Biochem. Biophys. Res. Commun. 190 (3): 1080–3. doi:10.1006/bbrc.1993.1159. PMID 8382485.
- York JD, Ponder JW, Majerus PW (May 1995). "Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure". Proc. Natl. Acad. Sci. U.S.A. 92 (11): 5149–53. doi:10.1073/pnas.92.11.5149. PMC 41866. PMID 7761465.
- Donahue JL, Bownas JL, Niehaus WG, Larson TJ (October 2000). "Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli". J. Bacteriol. 182 (19): 5624–7. doi:10.1128/jb.182.19.5624-5627.2000. PMC 111013. PMID 10986273.
- Stec B, Yang H, Johnson KA, Chen L, Roberts MF (November 2000). "MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase". Nat. Struct. Biol. 7 (11): 1046–50. doi:10.1038/80968. PMID 11062561.
- Rashid N, Imanaka H, Kanai T, Fukui T, Atomi H, Imanaka T (August 2002). "A novel candidate for the true fructose-1,6-bisphosphatase in archaea". J. Biol. Chem. 277 (34): 30649–55. doi:10.1074/jbc.M202868200. PMID 12065581.
- Nishimasu H, Fushinobu S, Shoun H, Wakagi T (June 2004). "The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea". Structure 12 (6): 949–59. doi:10.1016/j.str.2004.03.026. PMID 15274916.
- Fujita Y, Freese E (June 1979). "Purification and properties of fructose-1,6-bisphosphatase of Bacillus subtilis". J. Biol. Chem. 254 (12): 5340–9. PMID 221467.
- Fujita Y, Yoshida K, Miwa Y, Yanai N, Nagakawa E, Kasahara Y (August 1998). "Identification and expression of the Bacillus subtilis fructose-1, 6-bisphosphatase gene (fbp)". J. Bacteriol. 180 (16): 4309–13. PMC 107433. PMID 9696785.
- Berg, Jeremy Mark; John L. Tymoczko; Lubert Stryer (2002). "Glycolysis and Gluconeogenesis". In Susan Moran (ed.). Biochemistry (5th Edition ed.). 41 Madison Avenue, New York, New York: W. H. Freeman and Company. ISBN 0-7167-3051-0.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Fructose-1-6-bisphosphatase Provide feedback
No Pfam abstract.
Weeks CM, Roszak AW, Erman M, Kaiser R, Jornvall H, Ghosh D; , Acta Crystallogr D Biol Crystallogr 1999;55:93-102.: Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution. PUBMED:10089399 EPMC:10089399
Internal database links
|SCOOP:||Inositol_P FBPase_glpX Fve NdhM|
|Similarity to PfamA using HHSearch:||Inositol_P|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000146
This entry represents the fructose-1,6-bisphosphatase (FBPase) class 1 family. FBPase is a critical regulatory enzyme in gluconeogenesis that catalyses the removal of 1-phosphate from fructose 1,6-bis-phosphate to form fructose 6-phosphate [PUBMED:2159755, PUBMED:3008716]. It is involved in many different metabolic pathways and found in most organisms. FBPase requires metal ions for catalysis (Mg2+ and Mn2+ being preferred) and the enzyme is potently inhibited by Li+. The fold of fructose-1,6-bisphosphatase was noted to be identical to that of inositol-1-phosphatase (IMPase) [PUBMED:8382485]. Inositol polyphosphate 1-phosphatase (IPPase), IMPase and FBPase share a sequence motif (Asp-Pro-Ile/Leu-Asp-Gly/Ser-Thr/Ser) which has been shown to bind metal ions and participate in catalysis. This motif is also found in the distantly-related fungal, bacterial and yeast IMPase homologues. It has been suggested that these proteins define an ancient structurally conserved family involved in diverse metabolic pathways, including inositol signalling, gluconeogenesis, sulphate assimilation and possibly quinone metabolism [PUBMED:7761465].
This entry also includes sedoheptulose-1,7-bisphosphatase, which is a member of the FBPase class 1 family.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||phosphoric ester hydrolase activity (GO:0042578)|
|fructose 1,6-bisphosphate 1-phosphatase activity (GO:0042132)|
|Biological process||carbohydrate metabolic process (GO:0005975)|
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The graphic that is shown by default represents the longest sequence with a given architecture. Each row contains the following information:
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Members of this clan show metal-dependent / lithium sensitive phosphomonoesterase activity. The clan includes inositol polyphosphate 1 phosphatase and fructose 1,6-bisphosphatase .
The clan contains the following 3 members:FBPase FBPase_glpX Inositol_P
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Author:||Finn RD, Griffiths-Jones SR|
|Number in seed:||9|
|Number in full:||8884|
|Average length of the domain:||312.30 aa|
|Average identity of full alignment:||48 %|
|Average coverage of the sequence by the domain:||96.04 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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Unmapped species names
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the FBPase domain has been found. There are 226 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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