DB code: S00026

CATH domain 1.10.600.10 : Farnesyl Diphosphate Synthase Catalytic domain
E.C. 4.2.3.9
CSA 1di1
M-CSA 1di1
MACiE M0261

CATH domain Related DB codes (homologues)
1.10.600.10 : Farnesyl Diphosphate Synthase S00024 S00027

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
Q03471 Aristolochene synthase
AS
EC 4.2.3.9
Sesquiterpene cyclase
PF03936 (Terpene_synth_C)
[Graphical View]

KEGG enzyme name
aristolochene synthase
sesquiterpene cyclase
trans,trans-farnesyl diphosphate aristolochene-lyase
trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,aristolochene-forming)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q03471 ARIS_PENRO 2-trans,6-trans-farnesyl diphosphate = aristolochene + diphosphate. Cytoplasm. Magnesium. Manganese.

KEGG Pathways
Map code Pathways E.C.
MAP00900 Terpenoid biosynthesis

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00034 C00448 C02004 C00013
E.C.
Compound Magnesium Manganese trans,trans-farnesyl diphosphate Aristolochene diphosphate
Type divalent metal (Ca2+, Mg2+) heavy metal lipid,phosphate group/phosphate ion lipid phosphate group/phosphate ion
ChEBI 18420
18291
35154
17407
43445
29888
PubChem 888
23930
445713
656496
1023
21961011
1dgpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:FOH Unbound Unbound
1dgpB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:FOH Unbound Unbound
1di1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1di1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dgpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 92
1dgpB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 92
1di1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 92
1di1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 92

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
SCHEME I
[4]
Fig.5, Fig.6 3
[5]
Scheme 1 p.7742

References
[1]
Resource
Comments
Medline ID
PubMed ID 7986100
Journal Arch Biochem Biophys
Year 1994
Volume 315
Pages 527-32
Authors Back K, Yin S, Chappell J
Title Expression of a plant sesquiterpene cyclase gene in Escherichia coli.
Related PDB
Related UniProtKB
[2]
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
[3]
Resource
Comments
Medline ID
PubMed ID 9324768
Journal Science
Year 1997
Volume 277
Pages 1788-9
Authors Sacchettini JC, Poulter CD
Title Creating isoprenoid diversity.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 20400487
PubMed ID 10825154
Journal J Biol Chem
Year 2000
Volume 275
Pages 25533-9
Authors Caruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW
Title Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti.
Related PDB 1dgp 1di1
Related UniProtKB Q03471
[5]
Resource
Comments
Medline ID
PubMed ID 12820883
Journal Biochemistry
Year 2003
Volume 42
Pages 7741-7
Authors Deligeorgopoulou A, Allemann RK
Title Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-beta-farnesene synthase.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-05-24 2009-02-26