×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.190.80
Functional Family Fructose-1,6-bisphosphatase/inositol-1-monophosphatase

Enzyme Information

3.1.3.11
Fructose-bisphosphatase.
based on mapping to UniProt O33832
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate.
-!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
3.1.3.25
Inositol-phosphate phosphatase.
based on mapping to UniProt O33832
Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.
-!- Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. -!- It also acts on adenosine 2'-phosphate (but not the 3'- or 5'-phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate, but does not act on inositol bisphosphates or more phosphorylated inositols.

UniProtKB Entries (1)

O33832
BSUHB_THEMA
Thermotoga maritima MSB8
Fructose-1,6-bisphosphatase/inositol-1-monophosphatase

PDB Structure

PDB 2P3V
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima.
Stieglitz, K.A., Roberts, M.F., Li, W., Stec, B.
Febs J.
CATH-Gene3D is a Global Biodata Core Resource Learn more...