ID   CYC1_KITGR              Reviewed;         499 AA.
AC   Q9AJE4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Terpentedienyl-diphosphate synthase;
DE            EC=5.5.1.15;
GN   Name=cyc1;
OS   Kitasatospora griseola (Streptomyces griseolosporeus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=2064;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MF730-N6;
RX   PubMed=11567009; DOI=10.1128/jb.183.20.6085-6094.2001;
RA   Dairi T., Hamano Y., Kuzuyama T., Itoh N., Furihata K., Seto H.;
RT   "Eubacterial diterpene cyclase genes essential for production of the
RT   isoprenoid antibiotic terpentecin.";
RL   J. Bacteriol. 183:6085-6094(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, AND SUBUNIT.
RC   STRAIN=MF730-N6;
RX   PubMed=12138123; DOI=10.1074/jbc.m206382200;
RA   Hamano Y., Kuzuyama T., Itoh N., Furihata K., Seto H., Dairi T.;
RT   "Functional analysis of eubacterial diterpene cyclases responsible for
RT   biosynthesis of a diterpene antibiotic, terpentecin.";
RL   J. Biol. Chem. 277:37098-37104(2002).
CC   -!- FUNCTION: Involved in the production of the isoprenoid antibiotic
CC       terpentecin. Converts geranylgeranyl diphosphate (GGDP) into
CC       terpentedienol diphosphate (TDP) by a protonation-initiated
CC       cyclization. {ECO:0000269|PubMed:12138123}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = terpentedienyl
CC         diphosphate; Xref=Rhea:RHEA:25613, ChEBI:CHEBI:58756,
CC         ChEBI:CHEBI:58821; EC=5.5.1.15;
CC         Evidence={ECO:0000269|PubMed:12138123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:12138123};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=64.2 uM for GGDP {ECO:0000269|PubMed:12138123};
CC         Vmax=94.7 nmol/min/mg enzyme {ECO:0000269|PubMed:12138123};
CC       pH dependence:
CC         Optimum pH is 6.8. {ECO:0000269|PubMed:12138123};
CC       Temperature dependence:
CC         Optimum temperature is 25-30 degrees Celsius.
CC         {ECO:0000269|PubMed:12138123};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:11567009,
CC       ECO:0000269|PubMed:12138123}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12138123}.
CC   -!- DISRUPTION PHENOTYPE: Mutants do not produce terpentecin.
CC       {ECO:0000269|PubMed:11567009}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AB048795; BAB39206.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AJE4; -.
DR   SMR; Q9AJE4; -.
DR   STRING; 2064.TR51_15710; -.
DR   KEGG; ag:BAB39206; -.
DR   GO; GO:0016872; F:intramolecular lyase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR032696; SQ_cyclase_C.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF00432; Prenyltrans; 1.
DR   Pfam; PF13243; SQHop_cyclase_C; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..499
FT                   /note="Terpentedienyl-diphosphate synthase"
FT                   /id="PRO_0000418817"
FT   MOTIF           284..287
FT                   /note="DXDD motif"
FT   BINDING         284
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
SQ   SEQUENCE   499 AA;  54163 MW;  8AA35407160171A8 CRC64;
     MKDRAADPVT KFSPSPYETG QFLRISERAD VGTPQIDYLL ATQRPDGLWG SVGFELVPTL
     GAVAGLSSRP EYADRAGVTD AVARACEKLW ELALGEGGLP KLPDTVASEI IVPSLIDLLS
     EVLQRHRPAV GGKAGQEQEF PSPPGANAEL WRQLSDRIAR GQAIPKTAWH TLEAFHPLPK
     QFAATVTPAA DGAVTCSPSS TAAWLSAVGT DAGASTRAYL DEAQSRYGGA IPMGSSMPYF
     EVLWVLNLVL KYFPDVPIPR EIIEEIAAGF SDSGIGGGPG LPPDGDDTAY ANLAGDKLGA
     PTHPEILMKF WAEDHFVSYP GEQTPSETVN AHALEYLNHL RMRRGITEFG AVEDACAEWV
     ISQQTEDGCW YDKWNVSPYY STAACVEALL DARKQDEPQL DSLRRAREWL LRHQTDSGGW
     GMAEPSPEET AYAVLALDLF ASRGGEGAEE CAAAISRAKE FFTDESRENP PLWMGKDLYT
     PFRIVDVTVM CGRAVVGRY