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Q55012

- PENA_STREX

UniProt

Q55012 - PENA_STREX

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Protein
Pentalenene synthase
Gene
penA
Organism
Streptomyces exfoliatus (Streptomyces hydrogenans)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate.1 Publication

Cofactori

Binds 3 magnesium ions per subunit By similarity.1 Publication

Kineticsi

  1. KM=310 nM for FPP1 Publication

pH dependencei

Optimum pH is 8.2-8.4.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Magnesium 1
Metal bindingi80 – 801Magnesium 2
Metal bindingi84 – 841Magnesium 1
Metal bindingi84 – 841Magnesium 2
Metal bindingi219 – 2191Magnesium 3
Metal bindingi223 – 2231Magnesium 3 By similarity
Metal bindingi227 – 2271Magnesium 3 By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. pentalenene synthase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16834.
BRENDAi4.2.3.7. 6094.
UniPathwayiUPA00171; UER00581.
UPA00974.

Names & Taxonomyi

Protein namesi
Recommended name:
Pentalenene synthase (EC:4.2.3.7)
Short name:
PS
Alternative name(s):
Pentalenolactone biosynthesis protein A
Sesquiterpene cyclase
Sesquiterpene synthase
Gene namesi
Name:penA
OrganismiStreptomyces exfoliatus (Streptomyces hydrogenans)
Taxonomic identifieri1905 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761F → A: Loss of activity. 1 Publication
Mutagenesisi77 – 771F → A: Loss of activity. 1 Publication
Mutagenesisi77 – 771F → Y: 20-fold decrease in activity and catalytic efficiency. 1 Publication
Mutagenesisi80 – 801D → E: 150-fold decrease in activity. 20-fold increase in Km for FPP. 1 Publication
Mutagenesisi81 – 811D → E: 50-fold decrease in activity. 9-fold increase in Km for FPP. 1 Publication
Mutagenesisi84 – 841D → E: 2.5-fold increase in activity. 7-fold increase in Km for FPP. 1 Publication
Mutagenesisi219 – 2191N → A: Loss of activity. 1 Publication
Mutagenesisi219 – 2191N → D: 60-fold decrease in activity. 55-fold increase in Km for FPP. 1 Publication
Mutagenesisi219 – 2191N → L: Loss of activity. 1 Publication
Mutagenesisi308 – 3092WH → FF: 12-fold decrease in activity. 25-fold decrease in catalytic efficiency. 2 Publications
Mutagenesisi308 – 3081W → F: 4-fold decrease in activity. 2-fold decrease in catalytic efficiency. 1 Publication
Mutagenesisi309 – 3091H → A: 3-fold decrease in activity. 2 Publications
Mutagenesisi309 – 3091H → C: 4-fold decrease in activity. 2 Publications
Mutagenesisi309 – 3091H → F: 17-fold decrease in activity. 5-fold increase in Km for FPP. 2 Publications
Mutagenesisi309 – 3091H → S: 3-fold decrease in activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 337336Pentalenene synthase
PRO_0000097092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi128 ↔ 136

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 246
Helixi28 – 325
Helixi39 – 468
Helixi50 – 578
Helixi64 – 8118
Helixi86 – 894
Helixi91 – 10212
Helixi103 – 1053
Helixi115 – 12814
Helixi133 – 15422
Helixi166 – 17611
Helixi179 – 19012
Helixi196 – 1994
Helixi202 – 22221
Helixi224 – 2296
Helixi236 – 2449
Helixi248 – 27932
Helixi284 – 29613
Helixi298 – 30811
Turni309 – 3113

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HM4X-ray3.47A/B2-337[»]
1HM7X-ray2.90A/B2-337[»]
1PS1X-ray2.60A/B1-337[»]
ProteinModelPortaliQ55012.
SMRiQ55012. Positions 7-311.

Miscellaneous databases

EvolutionaryTraceiQ55012.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi80 – 845DDXXD motif

Domaini

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

Sequence similaritiesi

Belongs to the terpene synthase family.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR005630. Terpene_synthase_metal-bd.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamiPF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q55012-1 [UniParc]FASTAAdd to Basket

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MPQDVDFHIP LPGRQSPDHA RAEAEQLAWP RSLGLIRSDA AAERHLRGGY    50
ADLASRFYPH ATGADLDLGV DLMSWFFLFD DLFDGPRGEN PEDTKQLTDQ 100
VAAALDGPLP DTAPPIAHGF ADIWRRTCEG MTPAWCARSA RHWRNYFDGY 150
VDEAESRFWN APCDSAAQYL AMRRHTIGVQ PTVDLAERAG RFEVPHRVFD 200
SAVMSAMLQI AVDVNLLLND IASLEKEEAR GEQNNMVMIL RREHGWSKSR 250
SVSHMQNEVR ARLEQYLLLE SCLPKVGEIY QLDTAEREAL ERYRTDAVRT 300
VIRGSYDWHR SSGRYDAEFA LAAGAQGYLE ELGSSAH 337
Length:337
Mass (Da):38,002
Last modified:January 23, 2007 - v4
Checksum:i417FCE6D8C4BB18C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181H → W AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05213 Unassigned DNA. Translation: AAA19131.1.
HQ292066 Genomic DNA. Translation: ADO85594.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05213 Unassigned DNA. Translation: AAA19131.1 .
HQ292066 Genomic DNA. Translation: ADO85594.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HM4 X-ray 3.47 A/B 2-337 [» ]
1HM7 X-ray 2.90 A/B 2-337 [» ]
1PS1 X-ray 2.60 A/B 1-337 [» ]
ProteinModelPortali Q55012.
SMRi Q55012. Positions 7-311.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00171 ; UER00581 .
UPA00974 .
BioCyci MetaCyc:MONOMER-16834.
BRENDAi 4.2.3.7. 6094.

Miscellaneous databases

EvolutionaryTracei Q55012.

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
InterProi IPR005630. Terpene_synthase_metal-bd.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF03936. Terpene_synth_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48576. SSF48576. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPENA_STREX
AccessioniPrimary (citable) accession number: Q55012
Secondary accession number(s): E3VWK6
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

All the mutants (1 Publication and 1 Publication) 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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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