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Q55012 (PENA_STREX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pentalenene synthase

Short name=PS
EC=4.2.3.7
Alternative name(s):
Pentalenolactone biosynthesis protein A
Sesquiterpene cyclase
Sesquiterpene synthase
Gene names
Name:penA
OrganismStreptomyces exfoliatus (Streptomyces hydrogenans)
Taxonomic identifier1905 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene, which is the hydrocarbon precursor of the pentalenolactone family of antibiotics produced by a variety of Streptomyces species. Ref.1

Catalytic activity

(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate. Ref.5

Cofactor

Binds 3 magnesium ions per subunit By similarity. Ref.1

Pathway

Sesquiterpene biosynthesis; pentalenene biosynthesis; pentalenene from farnesyl diphosphate: step 1/1.

Antibiotic biosynthesis; pentalenolactone biosynthesis.

Subunit structure

Monomer. Ref.1

Domain

The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.

Miscellaneous

All the mutants (Ref.3 and Ref.5) retained substantial pentalenene synthase activity accompanied by production of varying proportions of abortive cyclization products such as germacrene A, protoilludene and beta-caryophyllene. This is a true derailment or diversion of the normal cyclization reaction, and not simply the consequence of trapping of a normally cryptic, cationic intermediate.

Sequence similarities

Belongs to the terpene synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=310 nM for FPP Ref.1

pH dependence:

Optimum pH is 8.2-8.4.

Ontologies

Keywords
   Biological processAntibiotic biosynthesis
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

pentalenene synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 337336Pentalenene synthase
PRO_0000097092

Regions

Motif80 – 845DDXXD motif

Sites

Metal binding801Magnesium 1
Metal binding801Magnesium 2
Metal binding841Magnesium 1
Metal binding841Magnesium 2
Metal binding2191Magnesium 3
Metal binding2231Magnesium 3 By similarity
Metal binding2271Magnesium 3 By similarity

Amino acid modifications

Disulfide bond128 ↔ 136

Experimental info

Mutagenesis761F → A: Loss of activity. Ref.5
Mutagenesis771F → A: Loss of activity. Ref.5
Mutagenesis771F → Y: 20-fold decrease in activity and catalytic efficiency. Ref.5
Mutagenesis801D → E: 150-fold decrease in activity. 20-fold increase in Km for FPP. Ref.5
Mutagenesis811D → E: 50-fold decrease in activity. 9-fold increase in Km for FPP. Ref.5
Mutagenesis841D → E: 2.5-fold increase in activity. 7-fold increase in Km for FPP. Ref.5
Mutagenesis2191N → A: Loss of activity. Ref.5
Mutagenesis2191N → D: 60-fold decrease in activity. 55-fold increase in Km for FPP. Ref.5
Mutagenesis2191N → L: Loss of activity. Ref.5
Mutagenesis308 – 3092WH → FF: 12-fold decrease in activity. 25-fold decrease in catalytic efficiency. Ref.3 Ref.5
Mutagenesis3081W → F: 4-fold decrease in activity. 2-fold decrease in catalytic efficiency. Ref.5
Mutagenesis3091H → A: 3-fold decrease in activity. Ref.3 Ref.5
Mutagenesis3091H → C: 4-fold decrease in activity. Ref.3 Ref.5
Mutagenesis3091H → F: 17-fold decrease in activity. 5-fold increase in Km for FPP. Ref.3 Ref.5
Mutagenesis3091H → S: 3-fold decrease in activity. Ref.3 Ref.5
Sequence conflict1181H → W AA sequence Ref.1

Secondary structure

....................................... 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q55012 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 417FCE6D8C4BB18C

FASTA33738,002
        10         20         30         40         50         60 
MPQDVDFHIP LPGRQSPDHA RAEAEQLAWP RSLGLIRSDA AAERHLRGGY ADLASRFYPH 

        70         80         90        100        110        120 
ATGADLDLGV DLMSWFFLFD DLFDGPRGEN PEDTKQLTDQ VAAALDGPLP DTAPPIAHGF 

       130        140        150        160        170        180 
ADIWRRTCEG MTPAWCARSA RHWRNYFDGY VDEAESRFWN APCDSAAQYL AMRRHTIGVQ 

       190        200        210        220        230        240 
PTVDLAERAG RFEVPHRVFD SAVMSAMLQI AVDVNLLLND IASLEKEEAR GEQNNMVMIL 

       250        260        270        280        290        300 
RREHGWSKSR SVSHMQNEVR ARLEQYLLLE SCLPKVGEIY QLDTAEREAL ERYRTDAVRT 

       310        320        330 
VIRGSYDWHR SSGRYDAEFA LAAGAQGYLE ELGSSAH 

« Hide

References

[1]"Pentalenene synthase. Purification, molecular cloning, sequencing, and high-level expression in Escherichia coli of a terpenoid cyclase from Streptomyces UC5319."
Cane D.E., Sohng J.-K., Lamberson C.R., Rudnicki S.M., Wu Z., Lloyd M.D., Oliver J.S., Hubbard B.R.
Biochemistry 33:5846-5857(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28; 57-73; 96-120 AND 145-157, FUNCTION, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: UC5319.
[2]"Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone."
Zhu D., Seo M.J., Ikeda H., Cane D.E.
J. Am. Chem. Soc. 133:2128-2131(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: UC5319.
[3]"Pentalenene synthase. Histidine-309 is not required for catalytic activity."
Seemann M., Zhai G., Umezawa K., Cane D.E.
J. Am. Chem. Soc. 121:591-592(1999)
Cited for: MUTAGENESIS OF HIS-309.
[4]"Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology."
Lesburg C.A., Zhai G., Cane D.E., Christianson D.W.
Science 277:1820-1824(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[5]"Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis."
Seemann M., Zhai G., de Kraker J.-W., Paschall C.M., Christianson D.W., Cane D.E.
J. Am. Chem. Soc. 124:7681-7689(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF MUTANT LEU-219, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-76; PHE-77; ASP-80; ASP-81; ASP-84; ASN-219; 308-TRP-HIS-309; TRP-308 AND HIS-309.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05213 Unassigned DNA. Translation: AAA19131.1.
HQ292066 Genomic DNA. Translation: ADO85594.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HM4X-ray3.47A/B2-337[»]
1HM7X-ray2.90A/B2-337[»]
1PS1X-ray2.60A/B1-337[»]
ProteinModelPortalQ55012.
SMRQ55012. Positions 7-311.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16834.
BRENDA4.2.3.7. 6094.
UniPathwayUPA00171; UER00581.
UPA00974.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR005630. Terpene_synthase_metal-bd.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ55012.

Entry information

Entry namePENA_STREX
AccessionPrimary (citable) accession number: Q55012
Secondary accession number(s): E3VWK6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 79 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways