DB code: S00027

CATH domain 1.10.600.10 : Farnesyl Diphosphate Synthase Catalytic domain
E.C. 4.2.3.7
CSA 1ps1
M-CSA 1ps1
MACiE M0089

CATH domain Related DB codes (homologues)
1.10.600.10 : Farnesyl Diphosphate Synthase S00024 S00026

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
Q55012 Pentalenene synthase
PS
EC 4.2.3.7
Pentalenolactone biosynthesis protein A
Sesquiterpene cyclase
Sesquiterpene synthase
PF03936 (Terpene_synth_C)
[Graphical View]

KEGG enzyme name
pentalenene synthase
pentalenene synthetase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q55012 PTLS_STRS3 2-trans,6-trans-farnesyl diphosphate = pentalenene + diphosphate. Monomer. Magnesium.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00448 C00013 C01841
E.C.
Compound Magnesium 2-trans,6-trans-Farnesyl diphosphate Pyrophosphate Pentalenene
Type divalent metal (Ca2+, Mg2+) lipid,phosphate group/phosphate ion phosphate group/phosphate ion others
ChEBI 18420
17407
29888
PubChem 888
445713
1023
21961011
194140
1ps1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ps1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1hm4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1hm4B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1hm7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1hm7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;Q55012 & literature;[2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ps1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 309 ASP 80;ASP 84(Magnesium binding)
1ps1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm4B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 309 ASP 80;ASP 84(Magnesium binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.5, p.1823-1824 6
[3]
Fig.9C p.3350
[4]
Scheme 1, Scheme 2 5

References
[1]
Resource
Comments
Medline ID
PubMed ID 8563643
Journal Protein Sci
Year 1995
Volume 4
Pages 2436-8
Authors Lesburg CA, Lloyd MD, Cane DE, Christianson DW
Title Crystallization and preliminary X-ray diffraction analysis of recombinant pentalenene synthase.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID 97442534
PubMed ID 9295272
Journal Science
Year 1997
Volume 277
Pages 1820-4
Authors Lesburg CA, Zhai G, Cane DE, Christianson DW
Title Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.
Related PDB 1ps1
Related UniProtKB Q55012
[3]
Resource
Comments
Medline ID
PubMed ID 12135472
Journal Eur J Biochem
Year 2002
Volume 269
Pages 3339-54
Authors Liang PH, Ko TP, Wang AH
Title Structure, mechanism and function of prenyltransferases.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12083921
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 7681-9
Authors Seemann M, Zhai G, de Kraker JW, Paschall CM, Christianson DW, Cane DE
Title Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis.
Related PDB 1hm4 1hm7
Related UniProtKB

Comments
This enzyme was transferred from E.C. 4.6.1.5 to E.C. 4.2.3.7.

Created Updated
2004-03-24 2009-02-26