Literature summary for 3.1.3.37 extracted from

Cotton, C.; Kabasakal, B.; Miah, N.; Murray, J.
Structure of the dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase from Thermosynechococcus elongatus bound with sedoheptulose-7-phosphate (2015), Acta Crystallogr. Sect. F, 71, 1341-1345 .

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermosynechococcus vestitus
gene tll1276, recombinant expression in Escherichia coli strain KRX	Thermosynechococcus vestitus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme with bound sedoheptulose-7-phosphate in the absence of AMP, hanging drop vapour diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 50 mM Tris-HCl pH 7.9, 50 mM NaCl, 1 mM Mg-sedoheptulose-7-phosphate, and 0.2 M MgCl2, with 0.001 ml of reservoir solution containing 0.06 M Na HEPES pH 7.5, 0.12 M MgCl2, and 27% v/v PEG 400, and equilibration over 0.1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.34 A resolution	Thermosynechococcus vestitus
structure with sedoheptulose-7-phosphate bound and in the absence of AMP, space group I4122. In the absence of AMP, the AMP-binding region is disordered	Thermosynechococcus vestitus

Crystallization (Comment)

Organism

purified enzyme with bound sedoheptulose-7-phosphate in the absence of AMP, hanging drop vapour diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 50 mM Tris-HCl pH 7.9, 50 mM NaCl, 1 mM Mg-sedoheptulose-7-phosphate, and 0.2 M MgCl2, with 0.001 ml of reservoir solution containing 0.06 M Na HEPES pH 7.5, 0.12 M MgCl2, and 27% v/v PEG 400, and equilibration over 0.1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.34 A resolution

Thermosynechococcus vestitus

structure with sedoheptulose-7-phosphate bound and in the absence of AMP, space group I4122. In the absence of AMP, the AMP-binding region is disordered

Thermosynechococcus vestitus

Inhibitors

Inhibitors	Comment	Organism	Structure
AMP	a regulatory inhibitor, AMP-binding loop structure analysis	Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Thermosynechococcus vestitus	a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase	?	-	?
sedoheptulose 1,7-bisphosphate + H2O	Thermosynechococcus vestitus	-	sedoheptulose 7-phosphate + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermosynechococcus vestitus	Q8DJE9	-	-
Thermosynechococcus vestitus	Q8DJE9	bifunctional D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase, EC 3.1.3.11 and EC 3.1.3.37, respectively	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain KRX	Thermosynechococcus vestitus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase	Thermosynechococcus vestitus	?	-	?
sedoheptulose 1,7-bisphosphate + H2O	-	Thermosynechococcus vestitus	sedoheptulose 7-phosphate + phosphate	-	?

Subunits

Subunits	Comment	Organism
More	three-dimensional structure analysis and comparison to the Synechocystis sp. PCC 6803 enzyme structure	Thermosynechococcus vestitus

Synonyms

Synonyms	Comment	Organism
dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase	-	Thermosynechococcus vestitus
FBP/SBPase	-	Thermosynechococcus vestitus
More	cf. EC 3.1.3.11	Thermosynechococcus vestitus
tll1276	-	Thermosynechococcus vestitus

General Information

General Information	Comment	Organism
evolution	the FBP/SBPase found in Thermosynechococcus elongatus is a type II FBPase, a member of the larger Li+-sensitive phosphatase superfamily. It shares 80% sequence identity with the Synechocystis sp. PCC 6803 FBP/SBPase	Thermosynechococcus vestitus
additional information	active-site residue are Asp33, Glu57, Glu100, Thr102, Tyr131, Lys134, Arg176, Arg178, Asp198, Asp200, and Glu225	Thermosynechococcus vestitus
physiological function	bifunctional enzyme FBP/SBPase is unique in that it catalyses two separate reactions in the Calvin cycle, both of which are catalysed by separate enzymes in plants. The reactions catalysed by FBP/SBPase are important for Calvin cycle flux, as indicated by their high predicted metabolic control coefficients	Thermosynechococcus vestitus