Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Trichodiene Synthase Like

     ⌊ Family trichodiene synthase

  ⌊ FunctionalDomain trichodiene synthase (ID 136060)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onMarch 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Fusarium sporotrichioides Taxon ID: 5514 62738847
Fusarium sporotrichioides Taxon ID: 5514 62738846
Fusarium sporotrichioides Taxon ID: 5514 62738845
Show All

Uniprot

Protein NameAccessionEC Number Identifier
Trichodiene synthase {ECO:0000303|PubMed:3800398} P13513 TRI5_FUSSP (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQLLKVDP
KRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLEDSKDDPYPTMVNYFDDLQAG
REQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFGGFPGSHDYPQF
LRRMNGLGHCVGASLWPKEQFNERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQ
ISLVKNYVVSDEISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHL
CDRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQLANVRSKDVK
EVQKPFLSSIELVE
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
Superfamily CAR This EFD conserves 2/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
100 Glu (E) side chain MISMATCH: This residue does not match the specified amino acid type of D, and thus may not function in the same manner as other sequences in the superfamily
104 Asp (D) side chain None --
225 Asn (N) side chain None --
Subgroup CAR This EFD conserves 6/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
100 Glu (E) side chain MISMATCH: This residue does not match the specified amino acid type of D, and thus may not function in the same manner as other sequences in the subgroup
101 Asp (D) side chain Forms salt bridge with R544 that facilitates active site closure activation -- spectator ICS PubMed:21562622
225 Asn (N) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:11698643
229 Ser (S) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:9107034
232 Lys (K) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
233 Glu (E) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:11698643
304 Arg (R) side chain Forms salt bridge with D152 that facilitates active site closure; Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
Family CAR This EFD conserves 10/11 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
93 Tyr (Y) side chain Stabilizes positive charge on C7 of substrate via cation-pi interaction electrostatic stabiliser -- spectator ICS PubMed:11698643
100 Glu (E) side chain MISMATCH: This residue does not match the specified amino acid type of D, and thus may not function in the same manner as other sequences in the family
101 Asp (D) side chain Forms salt bridge with R304 that facilitates active site closure activation -- spectator ICS PubMed:21562622
182 Arg (R) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
225 Asn (N) side chain Coordinates with a third divalent metal ion metal ligand -- binding ICS PubMed:11698643
229 Ser (S) side chain Coordinates with a third divalent metal ion metal ligand -- binding ICS PubMed:11698643
232 Lys (K) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
233 Glu (E) side chain Coordinates with a third divalent metal ion metal ligand -- binding ICS PubMed:11698643
304 Arg (R) side chain Forms salt bridge with D101 that facilitates active site closure; Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
305 Tyr (Y) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
306 Arg (R) side chain None -- IME PubMed:11698643

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
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
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
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
Aug. 2, 2014, 11:14 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.