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 onJan. 14, 2017

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 NameAccessionEC Number IdentifierModel
Trichodiene synthase P13513 4.2.3.6 TRI5_FUSSP (Swiss-Prot) 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. The Superfamily domain, when present, is shown using underlining. 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 Location Family/Subgroup CAR Function Role Evidence Code Reference
93 Tyr (Y) side chain family Stabilizes positive charge on C7 of substrate via cation-pi interaction electrostatic stabiliser -- spectator ICS
100 Asp (D) side chain family Coordinates with two divalent metal ions metal ligand -- binding ICS
100 Asp (D) side chain subgroup Mg2+ ligand metal ligand -- binding ICS
101 Asp (D) side chain family Forms salt bridge with R304 that facilitates active site closure activation -- spectator ICS
101 Asp (D) side chain subgroup Forms salt bridge with R544 that facilitates active site closure activation -- spectator ICS
182 Arg (R) side chain family Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS
225 Asn (N) side chain subgroup Mg2+ ligand metal ligand -- binding ICS
225 Asn (N) side chain family Coordinates with a third divalent metal ion metal ligand -- binding ICS
229 Ser (S) side chain family Coordinates with a third divalent metal ion metal ligand -- binding ICS
229 Ser (S) side chain subgroup Mg2+ ligand metal ligand -- binding ICS
232 Lys (K) side chain subgroup Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS
232 Lys (K) side chain family Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS
233 Glu (E) side chain subgroup Mg2+ ligand metal ligand -- binding ICS
233 Glu (E) side chain family Coordinates with a third divalent metal ion metal ligand -- binding ICS
304 Arg (R) side chain family Forms salt bridge with D101 that facilitates active site closure; Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS
304 Arg (R) side chain subgroup Forms salt bridge with D152 that facilitates active site closure; Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS
305 Tyr (Y) side chain family Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS
306 Arg (R) side chain family None -- IME

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 20 2.85 Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
1JFA Trichodiene Synthase From Fusarium Sporotrichioides Trichodiene Synthase 20 2.5 1,2-Ethanediol CSA • PDB • PDBSum
1JFG Trichodiene Synthase From Fusarium Sporotrichioides Complexed With Diphosphate Trichodiene Synthase 20 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 20 2.95 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2AEL R304K Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4R)-7-Azabisabolene Trichodiene Synthase 19 2.5 Yes Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
2AET R304K Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4S)-7-Azabisabolene Trichodiene Synthase 19 2.75 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2AEK R304K Trichodiene Synthase Trichodiene Synthase 19 2.9 Yes Magnesium Ion • 1,2-Ethanediol CSA • PDB • PDBSum
2PS7 Y295F Trichodiene Synthase Trichodiene Synthase 19 2.35 Yes Magnesium Ion • 1,2-Ethanediol CSA • PDB • PDBSum
2PS8 Y295F Trichodiene Synthase: Complex With Mg And Pyrophosphate Trichodiene Synthase 19 2.67 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1YYQ Y305F Trichodiene Synthase Complexed With Pyrophosphate Trichodiene Synthase 19 2.1 Yes Magnesium Ion • Pyrophosphate 2- CSA • PDB • PDBSum
1YYS Y305F Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4S)-7-Azabisabolene Trichodiene Synthase 19 2.75 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1YYR Y305F Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4R)-7-Azabisabolene Trichodiene Synthase 19 2.5 Yes Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
1YJ4 Y305F Trichodiene Synthase Trichodiene Synthase 19 2.3 Yes 1,2-Ethanediol CSA • PDB • PDBSum
2PS5 N225D Trichodiene Synthase: Complex With Mg And Pyrophosphate Trichodiene Synthase 19 2.1 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2PS4 N225D Trichodiene Synthase Trichodiene Synthase 19 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 19 2.95 Yes Magnesium Ion
(4 more ⇓)
CSA • PDB • PDBSum
1KIZ D100E Trichodiene Synthase Complexed With Pyrophosphate Trichodiene Synthase 19 2.6 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1KIY D100E Trichodiene Synthase Trichodiene Synthase 19 2.4 Yes 1,2-Ethanediol CSA • PDB • PDBSum
1YYT D100E Trichodiene Synthase: Complex With Mg, Pyrophosphate, And (4R)-7-Azabisabolene Trichodiene Synthase 19 2.9 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2PS6 N225D/S229T Trichodiene Synthase Trichodiene Synthase 18 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 UniProtKB.

Curation History

Time Change Annotation Old Value New Value
Nov. 4, 2014, 4:24 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.