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
 18420
 		17407
 17407
 		29888
 29888
PubChem 888
 888
 		445713
 445713
 		1023
 21961011
 1023
 21961011
 		194140
 194140
1ps1A Unbound Unbound Unbound Unbound
1ps1B Unbound Unbound Unbound Unbound
1hm4A Unbound Unbound Unbound Unbound
1hm4B Unbound Unbound Unbound Unbound
1hm7A Unbound Unbound Unbound Unbound
1hm7B 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 HIS 309 ASP 80;ASP 84(Magnesium binding)
1ps1B HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm4A HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm4B HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm7A HIS 309 ASP 80;ASP 84(Magnesium binding)
1hm7B 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