CATH Classification

Domain Context

CATH Clusters

Superfamily Farnesyl Diphosphate Synthase
Functional Family

Enzyme Information

4.2.3.75
(-)-germacrene D synthase.
based on mapping to UniProt Q9X839
(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate.
-!- In Solidago canadensis the biosynthesis results in the pro-R hydrogen at C-1 of the farnesy diphosphate ending up at C-11 of the (-)- germacrene D. -!- With Streptomyces coelicolor the pro-S hydrogen at C-1 ends up at C-11 of the (-)-germacrene D. -!- Formerly EC 4.2.3.n13.
4.1.99.16
Geosmin synthase.
based on mapping to UniProt Q9X839
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H(2)O = (-)-geosmin + acetone.
-!- Geosmin is the cause of the characteristic smell of moist soil. -!- It is a bifunctional enzyme. -!- The N-terminal part of the enzyme is EC 4.2.3.22, germacradienol synthase, and forms germacradienol from FPP. -!- The C-terminal part of the enzyme catalyzes the conversion of germacradienol to geosmin via (1S,4aS,8aS)-8,10-dimethyl- 1,2,3,4,4a,5,6,8a-octahydronaphthalene.
4.2.3.22
Germacradienol synthase.
based on mapping to UniProt Q9X839
(2E,6E)-farnesyl diphosphate + H(2)O = (1E,4S,5E,7R)-germacra-1(10),5- dien-11-ol + diphosphate.
-!- H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. -!- Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. -!- Both products are formed from a common intermediate. -!- The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16), a widely occurring metabolite of many streptomycetes, bacteria and fungi. -!- Also catalyzes the reaction of EC 4.2.3.75.

UniProtKB Entries (1)

Q9X839
CYC2_STRCO
Streptomyces coelicolor A3(2)
Germacradienol/geosmin synthase

PDB Structure

PDB 5DW7
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with alpha alpha Domain Architecture That Catalyzes a Unique Cyclization-Fragmentation Reaction Sequence.
Harris, G.G., Lombardi, P.M., Pemberton, T.A., Matsui, T., Weiss, T.M., Cole, K.E., Koksal, M., Murphy, F.V., Vedula, L.S., Chou, W.K., Cane, D.E., Christianson, D.W.
Biochemistry
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