Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Trichodiene Synthase Like

     ⌊ Family trichodiene synthase

  ⌊ FunctionalDomain trichodiene synthase (ID 131457)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Fusarium venenatum Taxon ID: 56646 269979988 ACZ56402.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a D2JM53 D2JM53_9HYPO (TrEMBL)

Sequence

Length of Enzyme (full-length): 247 | Length of Functional Domain: 247

1       10        20        30        40        50        60

WVKVSKECMADLSIHYTYTLVLDDSSDDPYPAMMNYFNDLQAGREQAHPWWALVNEHFPN
VLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWP
KEQFDERGLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSDEITLHE
ALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHLCDHRYRLNEIYEKVKGQ
KTEDAQK
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 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
23 Asp (D) side chain None --
27 Asp (D) side chain None --
148 Asn (N) side chain None --
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
23 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:11698643
24 Asp (D) side chain Forms salt bridge with R544 that facilitates active site closure activation -- spectator ICS PubMed:21562622
148 Asn (N) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:11698643
152 Ser (S) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:9107034
155 Lys (K) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
156 Glu (E) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:11698643
227 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 11/11 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
16 Tyr (Y) side chain Stabilizes positive charge on C7 of substrate via cation-pi interaction electrostatic stabiliser -- spectator ICS PubMed:11698643
23 Asp (D) side chain Coordinates with two divalent metal ions metal ligand -- binding ICS PubMed:11698643
24 Asp (D) side chain Forms salt bridge with R304 that facilitates active site closure activation -- spectator ICS PubMed:21562622
105 Arg (R) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
148 Asn (N) side chain Coordinates with a third divalent metal ion metal ligand -- binding ICS PubMed:11698643
152 Ser (S) side chain Coordinates with a third divalent metal ion metal ligand -- binding ICS PubMed:11698643
155 Lys (K) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
156 Glu (E) side chain Coordinates with a third divalent metal ion metal ligand -- binding ICS PubMed:11698643
227 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
228 Tyr (Y) side chain Interacts with substrate diphosphate to trigger substrate ionization electrostatic stabiliser -- spectator ICS PubMed:11698643
229 Arg (R) side chain None -- IME PubMed:11698643

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group 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
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, 1:07 p.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.