EzCatDB: S00027
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DB codeS00027
CATH domainDomain 11.10.600.10 : Farnesyl Diphosphate SynthaseCatalytic domain
E.C.4.2.3.7
CSA1ps1
MACiEM0089

CATH domainRelated DB codes (homologues)
1.10.600.10 : Farnesyl Diphosphate SynthaseS00024,S00026

Enzyme Name
UniProtKBKEGG

Q55012
Protein namePentalenene synthasepentalenene synthase
pentalenene synthetase
SynonymsPS
EC 4.2.3.7
Pentalenolactone biosynthesis protein A
Sesquiterpene cyclase
Sesquiterpene synthase
PfamPF03936 (Terpene_synth_C)
[Graphical view]


UniProtKB:Accession NumberQ55012
Entry namePTLS_STRS3
Activity2-trans,6-trans-farnesyl diphosphate = pentalenene + diphosphate.
SubunitMonomer.
Subcellular location
CofactorMagnesium.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00448C00013C01841
CompoundMagnesium2-trans,6-trans-Farnesyl diphosphatePyrophosphatePentalenene
Typedivalent metal (Ca2+, Mg2+)lipid,phosphate group/phosphate ionphosphate group/phosphate ionothers
ChEBI18420
17407
29888

PubChem888
445713
21961011
1023
194140
            
1ps1AUnboundUnboundUnboundUnbound
1ps1BUnboundUnboundUnboundUnbound
1hm4AUnboundUnboundUnboundUnbound
1hm4BUnboundUnboundUnboundUnbound
1hm7AUnboundUnboundUnboundUnbound
1hm7BUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;Q55012 & literature;[2]
pdbCatalytic residuesCofactor-binding residues
          
1ps1AHIS 309
ASP 80;ASP 84(Magnesium binding)
1ps1BHIS 309
ASP 80;ASP 84(Magnesium binding)
1hm4AHIS 309
ASP 80;ASP 84(Magnesium binding)
1hm4BHIS 309
ASP 80;ASP 84(Magnesium binding)
1hm7AHIS 309
ASP 80;ASP 84(Magnesium binding)
1hm7BHIS 309
ASP 80;ASP 84(Magnesium binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.5, p.1823-18246
[3]Fig.9Cp.3350
[4]Scheme 1, Scheme 25

references
[1]
PubMed ID8563643
JournalProtein Sci
Year1995
Volume4
Pages2436-8
AuthorsLesburg CA, Lloyd MD, Cane DE, Christianson DW
TitleCrystallization and preliminary X-ray diffraction analysis of recombinant pentalenene synthase.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID97442534
PubMed ID9295272
JournalScience
Year1997
Volume277
Pages1820-4
AuthorsLesburg CA, Zhai G, Cane DE, Christianson DW
TitleCrystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.
Related PDB1ps1
Related UniProtKBQ55012
[3]
PubMed ID12135472
JournalEur J Biochem
Year2002
Volume269
Pages3339-54
AuthorsLiang PH, Ko TP, Wang AH
TitleStructure, mechanism and function of prenyltransferases.
[4]
PubMed ID12083921
JournalJ Am Chem Soc
Year2002
Volume124
Pages7681-9
AuthorsSeemann M, Zhai G, de Kraker JW, Paschall CM, Christianson DW, Cane DE
TitlePentalenene synthase. Analysis of active site residues by site-directed mutagenesis.
Related PDB1hm4,1hm7

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

createdupdated
2004-03-242009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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