Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Terpene Cyclase Like 2

     ⌊ Family pentalenene synthase

  ⌊ FunctionalDomain pentalenene synthase (ID 3642)

Superfamily Assignment Evidence Code(s) FSM
Family Assignment Evidence Code CFM
This entry was last updated onOct. 30, 2014

References to Other Databases

Genbank

SpeciesGIAccessionModel
Streptomyces exfoliatus 309753138 ADO85594.1 (Genbank) MB
Streptomyces sp. 451846 AAA19131.1 (Genbank) MB
Streptomyces exfoliatus 3114507 MB
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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. 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 10/10 Family-specific CRs and 7/7 Subgroup-specific CRs.
Position Amino Acid Family/Subgroup CAR Function Evidence Code Reference
80 Asp (D) Both Metal ligand ICS
173 Arg (R) Both Hydrogen bonds to PPi anion ICS
219 Asn (N) Both Metal ligand ICS
81 Asp (D) Subgroup Positions R794 ICS
223 Ser (S) Subgroup Metal ligand ICS
227 Glu (E) Subgroup Metal ligand ICS
314 Arg (R) Subgroup Hydrogen bonds to PPi anion ICS
76 Phe (F) Family Stabilizes carbocation intermediates through quadrupole-charge interactions ICS
77 Phe (F) Family Stabilizes carbocation intermediates through quadrupole-charge interactions ICS
84 Asp (D) Family Coordinates required divalent metal ICS
157 Arg (R) Family Stabilizes pyrophosphate leaving group ICS
226 Lys (K) Family Stabilizes pyrophosphate leaving group ICS
230 Arg (R) Family Stabilizes pyrophosphate leaving group ICS
308 Trp (W) Family Stabilizes carbocation intermediates through quadrupole-charge interactions ICS

Catalyzed Reaction(s)

pentalenene synthase

Evidence Code: IDA

EC: 4.2.3.7 | IntEnz: 4.2.3.7 | Kegg: 4.2.3.7 | BioCyc: 4.2.3.7 | BRENDA: 4.2.3.7 | MACiE: M0089 | EzCatDB: S00027

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.