PTLA_STRAW
ID PTLA_STRAW Reviewed; 336 AA.
AC Q82IY4;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=ptlA; OrderedLocusNames=SAV_2998;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=16681390; DOI=10.1021/bi060419n;
RA Tetzlaff C.N., You Z., Cane D.E., Takamatsu S., Omura S., Ikeda H.;
RT "A gene cluster for biosynthesis of the sesquiterpenoid antibiotic
RT pentalenolactone in Streptomyces avermitilis.";
RL Biochemistry 45:6179-6186(2006).
RN [4]
RP PATHWAY.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=21250661; DOI=10.1021/bi1019786;
RA Seo M.J., Zhu D., Endo S., Ikeda H., Cane D.E.;
RT "Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger
RT monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the
RT final steps of the biosynthesis of pentalenolactone and
RT neopentalenolactone.";
RL Biochemistry 50:1739-1754(2011).
CC -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to
CC the tricyclic sesquiterpene pentalenene in the biosynthesis of
CC neopentalenolactone antibiotic. {ECO:0000269|PubMed:16681390}.
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 Evidence={ECO:0000269|PubMed:16681390};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for farnesyl diphosphate {ECO:0000269|PubMed:16681390};
CC Note=kcat is 0.605 sec(-1).;
CC -!- PATHWAY: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
CC {ECO:0000269|PubMed:21250661}.
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 -!- MISCELLANEOUS: S.avermitilis does not produce pentalenolactone itself
CC in vivo but instead a group of new metabolites that are
CC neopentalenolactone derivatives. {ECO:0000305|PubMed:21250661}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; BA000030; BAC70709.1; -; Genomic_DNA.
DR RefSeq; WP_010984429.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82IY4; -.
DR SMR; Q82IY4; -.
DR STRING; 227882.SAV_2998; -.
DR EnsemblBacteria; BAC70709; BAC70709; SAVERM_2998.
DR KEGG; sma:SAVERM_2998; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_042538_4_0_11; -.
DR OMA; AMEHWVI; -.
DR OrthoDB; 1869158at2; -.
DR BioCyc; MetaCyc:MON-16846; -.
DR UniPathway; UPA01021; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050467; F:pentalenene synthase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901336; P:lactone biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Antibiotic biosynthesis; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..336
FT /note="Pentalenene synthase"
FT /id="PRO_0000422012"
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 336 AA; 37897 MW; 953DBA6E0F4B217D CRC64;
MPQDVDFHIP FPSRRSPDFE RARADHLSWP RALGLIGTDA AAERHSRGGY ADLAARFYPS
ATGADLDLGV DLMSWFFLFD DLFDGPRGED PQETRKLTDA VAAALDGPLP TSAPPIAHGF
ADVWRRTCQG MSPAWRARSA RHWRNYFSGY VDEAVSRHLN TPYDSAGHYL AMRRQTIGVQ
PTVDLAERSC HCEVPQRVFD SAVLFAMLQI ATDTNLILND IASLEKEEAR GELNNMVFIL
MREHGWTRGR SIAHMQDGVR TRLEQFLLLE ACLPKVYDTF ELTAQERESA EKYRMDGVRS
VIRGSYDWHR SSGRYAADYA IAASYQGYLE ELGSTL
