Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Terpene Cyclase Like 2

     ⌊ Family   private

  ⌊ FunctionalDomain pentalenene synthase (ID 130584)

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
Streptomyces exfoliatus Taxon ID: 1905 23200135
Streptomyces exfoliatus Taxon ID: 1905 23200134
Streptomyces exfoliatus Taxon ID: 1905 23200133
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Uniprot

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

Sequence

Length of Enzyme (full-length): 336 | Length of Functional Domain: 336

1       10        20        30        40        50        60

PQDVDFHIPLPGRQSPDHARAEAEQLAWPRSLGLIRSDAAAERHLRGGYADLASRFYPHA
TGADLDLGVDLMSWFFLFDDLFDGPRGENPEDTKQLTDQVAAALDGPLPDTAPPIAHGFA
DIWRRTCEGMTPAWCARSARHWRNYFDGYVDEAESRFWNAPCDSAAQYLAMRRHTIGVQP
TVDLAERAGRFEVPHRVFDSAVMSAMLQIAVDVNLLLLDIASLEKEEARGEQNNMVMILR
REHGWSKSRSVSHMQNEVRARLEQYLLLESCLPKVGEIYQLDTAEREALERYRTDAVRTV
IRGSYDWHRSSGRYDAEFALAAGAQGYLEELGSSAH
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
79 Asp (D) side chain None --
83 Asp (D) side chain None --
218 Leu (L) side chain MISMATCH: This residue does not match the specified amino acid type of D,N, and thus may not function in the same manner as other sequences in the superfamily
Subgroup CAR This EFD conserves 7/8 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
79 Asp (D) side chain Metal ligand metal ligand -- binding ICS PubMed:20131801
80 Asp (D) side chain Forms hydrogen bond with R767 that facilitates active site closure activation -- spectator ICS PubMed:21562622
172 Arg (R) side chain Hydrogen bonds to PPi anion electrostatic stabiliser -- spectator ICS PubMed:20131801
218 Leu (L) side chain MISMATCH: This residue does not match the specified amino acid type of N, and thus may not function in the same manner as other sequences in the subgroup
219 Asp (D) side chain None -- ISS
222 Ser (S) side chain Metal ligand metal ligand -- binding ICS PubMed:20131801
226 Glu (E) side chain Metal ligand metal ligand -- binding ICS PubMed:20131801
313 Arg (R) side chain Forms hydrogen bond with D219 that facilitates active site closure; Hydrogen bonds to PPi anion activation -- spectator ICS PubMed:21562622
Family CAR This EFD conserves 9/10 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
75 Phe (F) side chain Stabilizes carbocation intermediates through quadrupole-charge interactions electrostatic stabiliser -- spectator ICS PubMed:9295272
76 Phe (F) side chain Stabilizes carbocation intermediates through quadrupole-charge interactions electrostatic stabiliser -- spectator ICS PubMed:9295272
79 Asp (D) side chain Coordinates required divalent metal metal ligand -- binding ICS PubMed:9295272
83 Asp (D) side chain Coordinates required divalent metal metal ligand -- binding ICS PubMed:9295272
156 Arg (R) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS PubMed:9295272
172 Arg (R) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS PubMed:9295272
218 Leu (L) main chain carbonyl group MISMATCH: This residue does not match the specified amino acid type of N, and thus may not function in the same manner as other sequences in the family
225 Lys (K) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS PubMed:9295272
229 Arg (R) side chain Stabilizes pyrophosphate leaving group electrostatic stabiliser -- spectator ICS PubMed:9295272
307 Trp (W) side chain Stabilizes carbocation intermediates through quadrupole-charge interactions electrostatic stabiliser -- spectator ICS PubMed:9295272

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
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
1PS1 Pentalenene Synthase Pentalenene Synthase 2 2.6 Trimethyl Lead Ion 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 p.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.