Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Trichodiene Synthase Like

     ⌊ Family trichodiene synthase

  ⌊ FunctionalDomain trichodiene synthase (ID 3643)

Superfamily Assignment Evidence Code(s) FSM
Family Assignment Evidence Code CFM
This entry was last updated onJuly 31, 2014

Related Enzyme Functional Domain(s)

uncharacterized ISI.BS proteingroup sequence

References to Other Databases

Genbank

SpeciesGIAccessionModel
Fusarium sporotrichioides 15054400 AAK77935.1 (Genbank) MB
Fusarium sporotrichioides 13621069 AAK33074.1 (Genbank) MB
Fusarium sporotrichioides 168160 AAD13657.1 (Genbank) MB
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Uniprot

Protein NameAccessionIdentifierModel
Trichodiene synthase P13513 TRI5_FUSSP (SwissProt) MB
n/a Q7LP67 Q7LP67_FUSSP (Trembl) MB

Sequence

Length of Enzyme (full-length): 374 | Length of Functional Domain: 374

1       10        20        30        40        50        60

MENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQLLKVDP
KRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSKDDPYPTMVNYFDDLQAG
REQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFGGFPGSHDYPQF
LRRMNGLGHCVGASLWPKEQFNERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQ
ISLVKNYVVSDEISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHL
CDRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQLANVRSKDVK
EVQKPFLSSIELVE

FASTA | BLAST | HMM

This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. In many cases the functional domain is the full-length sequence. Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

This EFD conserves 11/11 Family-specific CRs and 7/7 Subgroup-specific CRs.
Position Amino Acid Family/Subgroup CAR Function Evidence Code Reference
100 Asp (D) Both Mg2+ ligand ICS
101 Asp (D) Both None IME
225 Asn (N) Both Mg2+ ligand ICS
229 Ser (S) Both Mg2+ ligand ICS
232 Lys (K) Both Interacts with substrate diphosphate to trigger substrate ionization ICS
233 Glu (E) Both Mg2+ ligand ICS
304 Arg (R) Both Interacts with substrate diphosphate to trigger substrate ionization ICS
93 Tyr (Y) Family Stabilizes positive charge on C7 of substrate via cation-pi interaction ICS
182 Arg (R) Family Interacts with substrate diphosphate to trigger substrate ionization ICS
305 Tyr (Y) Family Interacts with substrate diphosphate to trigger substrate ionization ICS
306 Arg (R) Family None IME

Catalyzed Reaction(s)

trichodiene synthase

Evidence Code: IDA

EC: 4.2.3.6 | IntEnz: 4.2.3.6 | Kegg: 4.2.3.6 | BioCyc: 4.2.3.6 | BRENDA: 4.2.3.6

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Chimera Session Links
2Q9Y Trichodiene Synthase: Complex With Mg, Inorganic Pyrophosphate, And Benzyl Triethyl Ammonium Cation Trichodiene Synthase 40 2.85 Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
1JFA Trichodiene Synthase From Fusarium Sporotrichioides Trichodiene Synthase 40 2.5 1,2-Ethanediol CSA • PDB • PDBSum
1JFG Trichodiene Synthase From Fusarium Sporotrichioides Complexed With Diphosphate Trichodiene Synthase 40 2.5 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2Q9Z Trichodiene Synthase: Complex With Inorganic Pyrophosphate Resulting From The Reaction With 2-Fluorofarnesyl Diphosphate Trichodiene Synthase 40 2.95 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2AEL R304K Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4R)-7-Azabisabolene Trichodiene Synthase 38 2.5 Yes Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
2AET R304K Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4S)-7-Azabisabolene Trichodiene Synthase 38 2.75 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2AEK R304K Trichodiene Synthase Trichodiene Synthase 38 2.9 Yes Magnesium Ion • 1,2-Ethanediol CSA • PDB • PDBSum
2PS7 Y295F Trichodiene Synthase Trichodiene Synthase 38 2.35 Yes Magnesium Ion • 1,2-Ethanediol CSA • PDB • PDBSum
2PS8 Y295F Trichodiene Synthase: Complex With Mg And Pyrophosphate Trichodiene Synthase 38 2.67 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1YYQ Y305F Trichodiene Synthase Complexed With Pyrophosphate Trichodiene Synthase 38 2.1 Yes Magnesium Ion • Pyrophosphate 2- CSA • PDB • PDBSum
1YYS Y305F Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4S)-7-Azabisabolene Trichodiene Synthase 38 2.75 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1YYR Y305F Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4R)-7-Azabisabolene Trichodiene Synthase 38 2.5 Yes Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
1YJ4 Y305F Trichodiene Synthase Trichodiene Synthase 38 2.3 Yes 1,2-Ethanediol CSA • PDB • PDBSum
2PS5 N225D Trichodiene Synthase: Complex With Mg And Pyrophosphate Trichodiene Synthase 38 2.1 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2PS4 N225D Trichodiene Synthase Trichodiene Synthase 38 2.46 Yes Magnesium Ion • 1,2-Ethanediol CSA • PDB • PDBSum
1YYU D100E Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4S)-7-Azabisabolene Trichodiene Synthase 38 2.95 Yes Magnesium Ion
(4 more ⇓)
CSA • PDB • PDBSum
1KIZ D100E Trichodiene Synthase Complexed With Pyrophosphate Trichodiene Synthase 38 2.6 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1KIY D100E Trichodiene Synthase Trichodiene Synthase 38 2.4 Yes 1,2-Ethanediol CSA • PDB • PDBSum
1YYT D100E Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4R)-7-Azabisabolene Trichodiene Synthase 38 2.9 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2PS6 N225D/S229T Trichodiene Synthase Trichodiene Synthase 36 2.6 Yes 1,2-Ethanediol CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via Uniprot.