ID   PNTA_STRAE              Reviewed;         337 AA.
AC   E3VWJ0;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Pentalenene synthase;
DE            Short=PS;
DE            EC=4.2.3.7;
DE   AltName: Full=Pentalenolactone biosynthesis protein A;
DE   AltName: Full=Sesquiterpene cyclase;
DE   AltName: Full=Sesquiterpene synthase;
GN   Name=pntA;
OS   Streptomyces arenae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=29301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tu469;
RX   PubMed=21284395; DOI=10.1021/ja111279h;
RA   Zhu D., Seo M.J., Ikeda H., Cane D.E.;
RT   "Genome mining in streptomyces. Discovery of an unprecedented P450-
RT   catalyzed oxidative rearrangement that is the final step in the
RT   biosynthesis of pentalenolactone.";
RL   J. Am. Chem. Soc. 133:2128-2131(2011).
CC   -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to
CC       the tricyclic sesquiterpene pentalenene, which is the hydrocarbon
CC       precursor of the pentalenolactone family of antibiotics produced by a
CC       variety of Streptomyces species. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + pentalenene;
CC         Xref=Rhea:RHEA:18081, ChEBI:CHEBI:17251, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:175763; EC=4.2.3.7;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Sesquiterpene biosynthesis; pentalenene biosynthesis;
CC       pentalenene from farnesyl diphosphate: step 1/1.
CC   -!- PATHWAY: Antibiotic biosynthesis; pentalenolactone biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC       the catalytic activity, presumably through binding to Mg(2+).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ292065; ADO85578.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWJ0; -.
DR   SMR; E3VWJ0; -.
DR   UniPathway; UPA00171; UER00581.
DR   UniPathway; UPA00974; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050467; F:pentalenene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034686; Terpene_cyclase-like_2.
DR   SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..337
FT                   /note="Pentalenene synthase"
FT                   /id="PRO_0000422013"
FT   MOTIF           80..84
FT                   /note="DDXXD motif"
FT   BINDING         80
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  38063 MW;  986B53D95A8515B5 CRC64;
     MPQDVDFHIP LPGRQSPDFA RADAEQLAWP RSLGLINSEA AAERHLRGGY ADLASRFYPH
     ATGADLDLGV DLMSWFFLFD DLFDGPRGEN PQETKQLTDA VAAALDGPLP DTAPPIAHGF
     ADIWRRTSEG MTPAWCARSA RHWRSYFDGY VDEAESRFWD TPYDSAAQYL AVRRQTIGVQ
     PTVDLAERAG RFEVPHRVFD SAVLSAMLQI AVDVNLLLND IASLEKEEAR GEQNNMVMIL
     RREHGWSKDR SVAHIQSEVR VRLEQYLVLE SCLPQVGDIY RLDDAEREAL ERYRDDAVRT
     VIRGSYDWHR SSGRYDAEFA LAAGAQGYLE ELGRITH