ID   TASY_TAXBA              Reviewed;         862 AA.
AC   Q93YA3;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Taxadiene synthase;
DE            EC=4.2.3.17;
DE   AltName: Full=Taxa-4(5),11(12)-diene synthase;
GN   Name=TDC1; Synonyms=TASY;
OS   Taxus baccata (English yew).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Taxaceae;
OC   Taxus.
OX   NCBI_TaxID=25629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Goerhardt B.;
RL   Thesis (2001), Technische Universitaet Berlin, Germany.
CC   -!- FUNCTION: Catalyzes the cyclization of the ubiquitous isoprenoid
CC       intermediate geranylgeranyl diphosphate to taxa-4,11-diene, the parent
CC       olefin with a taxane skeleton.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + taxa-
CC         4,11-diene; Xref=Rhea:RHEA:20912, ChEBI:CHEBI:30037,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58756; EC=4.2.3.17;
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: Alkaloid biosynthesis; taxol biosynthesis; taxa-4(20),11-dien-
CC       5alpha-ol from geranylgeranyl diphosphate: step 1/2.
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   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AJ320538; CAC42773.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93YA3; -.
DR   SMR; Q93YA3; -.
DR   BRENDA; 4.2.3.17; 6222.
DR   UniPathway; UPA00842; UER00806.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050553; F:taxadiene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0042617; P:paclitaxel biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR   InterPro; IPR001906; Terpene_synth_N.
DR   InterPro; IPR036965; Terpene_synth_N_sf.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; SSF48239; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding; Taxol biosynthesis.
FT   CHAIN           1..862
FT                   /note="Taxadiene synthase"
FT                   /id="PRO_0000186449"
FT   MOTIF           613..617
FT                   /note="DDXXD motif"
FT   BINDING         613
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         613
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         617
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         617
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         757
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         761
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         765
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   862 AA;  98049 MW;  B37835AFFDC1DEFE CRC64;
     MAQLSFNAAL KMNALGNKAI HDPTNCRAKS ERQMMWVCSR SGRTRVKMSR GSGGPGPVVM
     MSSSTGTSKV VSETSSTIVD DIPRLSANYH GDLWHHNVIQ TLETPFRESS TYQERADELV
     VKIKDMFNAL GDGDISPSAY DTAWVARVAT VSSDGSEKPR FPQALNWVLN NQLQDGSWGI
     ESHFSLCDRL LNTVNSVIAL SVWKTGHSQV EQGAEFIAEN LRLLNEEDEL SPDFEIIFPA
     LLQKAKALGI NLPYDLPFIK SLSTTREARL TDVSAAADNI PANMLNALEG LEEVIDWNKI
     MRFQSKDGSF LSSPASTACV LMNTGDEKCF TLLNNLLDKF GGCVPCMYSI DLLERLSLVD
     NIEHLGIGRH FKQEIKVALD YVYRHWSERG IGWGRDSLVP DLNTTALGLR TLRTHGYDVS
     SDVLNNFKDE NGRFFSSAGQ THVELRSVVN LFRASDLAFP DEGAMDDARK FAEPYLRDAL
     ATKISTNTKL YKEIEYVVEY PWHMSIPRLE ARSYIDSYDD DYVWQRKTLY RMPSLSNSKC
     LELAKLDFNI VQSLHQEELK LLTRWWKESG MADINFTRHR VAEVYFSSAT FEPEYSATRI
     AFTKIGCLQV LFDDMADIFA TLDELKSFTE GVKRWDTSLL HEIPECMQTC FKVWFKLMEE
     VNNDVVKVQG RDMLAHIRKP WELYFNCYVQ EREWLEAGYI PTFEEYLKTY AISVGLGPCT
     LQPILLMGEL VKDDVVEKVH YPSNMFELVS LSWRLTNDTK TYQAEKARGQ QASGIACYMK
     DNPGATEEDA IKHICRVVDR ALKEASFEYF KPSNDIPMGC KSFIFNLRLC VQIFYKFIDG
     YGIANEEIKD YIRKVYIDPI QV