Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Terpene Cyclase Like 2

     ⌊ Family   private

  ⌊ FunctionalDomain pentalenene synthase (ID 3642)

Superfamily Assignment Evidence Code(s) FSM
Family Assignment Evidence Code CFM
This entry was last updated onApril 1, 2017

References to Other Databases

Genbank

SpeciesGIAccessionModel
Streptomyces exfoliatus 309753138 ADO85594.1 (Genbank) MB
Streptomyces sp. 451846 AAA19131.1 (Genbank) MB
Streptomyces exfoliatus 3114507 MB
Show All

Uniprot

Protein NameAccessionEC Number IdentifierModel
Pentalenene synthase Q55012 4.2.3.7 PENA_STREX (Swiss-Prot) MB

Sequence

Length of Enzyme (full-length): 337 | Length of Functional Domain: 337

1       10        20        30        40        50        60

MPQDVDFHIPLPGRQSPDHARAEAEQLAWPRSLGLIRSDAAAERHLRGGYADLASRFYPH
ATGADLDLGVDLMSWFFLFDDLFDGPRGENPEDTKQLTDQVAAALDGPLPDTAPPIAHGF
ADIWRRTCEGMTPAWCARSARHWRNYFDGYVDEAESRFWNAPCDSAAQYLAMRRHTIGVQ
PTVDLAERAGRFEVPHRVFDSAVMSAMLQIAVDVNLLLNDIASLEKEEARGEQNNMVMIL
RREHGWSKSRSVSHMQNEVRARLEQYLLLESCLPKVGEIYQLDTAEREALERYRTDAVRT
VIRGSYDWHRSSGRYDAEFALAAGAQGYLEELGSSAH

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

Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
80 Asp (D) side chain None --
84 Asp (D) side chain None --
219 Asn (N) side chain None --
Subgroup CAR This EFD conserves 8/8 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
80 Asp (D) side chain Metal ligand metal ligand -- binding ICS
81 Asp (D) side chain Forms hydrogen bond with R767 that facilitates active site closure activation -- spectator ICS
173 Arg (R) side chain Hydrogen bonds to PPi anion electrostatic stabiliser -- spectator ICS
219 Asn (N) side chain Metal ligand metal ligand -- binding ICS
220 Asp (D) side chain None -- ISS
223 Ser (S) side chain Metal ligand metal ligand -- binding ICS
227 Glu (E) side chain Metal ligand metal ligand -- binding ICS
314 Arg (R) side chain Forms hydrogen bond with D219 that facilitates active site closure; Hydrogen bonds to PPi anion activation -- spectator ICS
Family CAR This EFD conserves 10/10 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
76 Phe (F) side chain Stabilizes carbocation intermediates through quadrupole-charge interactions electrostatic stabiliser -- spectator ICS
77 Phe (F) side chain Stabilizes carbocation intermediates through quadrupole-charge interactions electrostatic stabiliser -- spectator ICS
80 Asp (D) side chain Coordinates required divalent metal metal ligand -- binding ICS
84 Asp (D) side chain Coordinates required divalent metal metal ligand -- binding ICS
157 Arg (R) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS
173 Arg (R) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS
219 Asn (N) main chain carbonyl group Backbone carbonyl stabilizes carbocation intermediate through dipole-charge interaction electrostatic stabiliser -- spectator ICS
226 Lys (K) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS
230 Arg (R) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS
308 Trp (W) side chain Stabilizes carbocation intermediates through quadrupole-charge interactions electrostatic stabiliser -- spectator ICS

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Chimera Session Links
1PS1 Pentalenene Synthase Pentalenene Synthase 2 2.6 Trimethyl Lead Ion CSA • PDB • PDBSum
1HM4 N219L Pentalenene Synthase Pentalenene Synthase 2 3.47 Yes CSA • PDB • PDBSum
1HM7 N219L Pentalenene Synthase Pentalenene Synthase 2 2.9 Yes 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
April 30, 2014, 11:58 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 328 337
EC number assigned by UniProtKB accession ID.