Fructose 1,6-bisphosphatase

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The enzyme fructose bisphosphatase (EC 3.1.3.11; systematic name D-fructose-1,6-bisphosphate 1-phosphohydrolase) catalyses the conversion of fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis and the Calvin cycle, which are both anabolic pathways:[1][2]

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
Quick facts: fructose-1,6-bisphosphatase 1, Identifiers, S...
fructose-1,6-bisphosphatase 1
Fructose-1.6-bisphosphatase-pdb-3FBP.png
Fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex. Rendered from PDB 3FBP.
Identifiers
SymbolFBP1
Alt. symbolsFBP
NCBI gene2203
HGNC3606
OMIM229700
RefSeqNM_000507
UniProtP09467
Other data
EC number3.1.3.11
LocusChr. 9 q22.3
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StructuresSwiss-model
DomainsInterPro
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Quick facts: Fructose-1-6-bisphosphatase, Identifiers, Sym...
Fructose-1-6-bisphosphatase
PDB_1bk4_EBI.jpg
crystal structure of rabbit liver fructose-1,6-bisphosphatase at 2.3 angstrom resolution
Identifiers
SymbolFBPase
PfamPF00316
Pfam clanCL0171
InterProIPR000146
PROSITEPDOC00114
SCOP21frp / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
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Quick facts: Firmicute fructose-1,6-bisphosphatase, Identi...
Firmicute fructose-1,6-bisphosphatase
Identifiers
SymbolFBPase_2
PfamPF06874
Pfam clanCL0163
InterProIPR009164
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
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Quick facts: Fructose-1,6-bisphosphatase, Identifiers, Sym...
Fructose-1,6-bisphosphatase
1umg4.jpg
crystal structure of fructose-1,6-bisphosphatase
Identifiers
SymbolFBPase_3
PfamPF01950
InterProIPR002803
SCOP21umg / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
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Phosphofructokinase (EC 2.7.1.11) catalyses the reverse conversion of fructose 6-phosphate to fructose-1,6-bisphosphate, but this is not just the reverse reaction, because the co-substrates are different (and so thermodynamic requirements are not violated). The two enzymes each catalyse the conversion in one direction only, and are regulated by metabolites such as fructose 2,6-bisphosphate so that high activity of one of them 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+.