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 18420 |
18291 35154 18291 35154 |
17407 17407 |
43445 43445 |
29888 29888 |
||||||
| PubChem |
888 888 |
23930 23930 |
445713 445713 |
656496 656496 |
1023 21961011 1023 21961011 |
||||||
| 1dgpA |
|
|
|
|
|
Unbound | Unbound | Analogue:FOH | Unbound | Unbound | |
| 1dgpB |
|
|
|
|
|
Unbound | Unbound | Analogue:FOH | Unbound | Unbound | |
| 1di1A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1di1B |
|
|
|
|
|
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 |
|
|
|
|
|
TYR 92 | ||||
| 1dgpB |
|
|
|
|
|
TYR 92 | ||||
| 1di1A |
|
|
|
|
|
TYR 92 | ||||
| 1di1B |
|
|
|
|
|
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, |
| 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 |