TASY_TAXWC
ID TASY_TAXWC Reviewed; 862 AA.
AC Q9FT37;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Taxadiene synthase;
DE EC=4.2.3.17;
DE AltName: Full=Taxa-4(5),11(12)-diene synthase;
GN Name=TDC1;
OS Taxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Taxaceae;
OC Taxus.
OX NCBI_TaxID=29808;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Callus;
RA Wang W., Shi Q., Ouyang T., Zhu P., Cheng K.;
RT "Cloning, expression, and characterization of taxadiene synthase, a
RT diteroene cyclase from Taxus chinensis.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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; AY007207; AAG02257.1; -; mRNA.
DR AlphaFoldDB; Q9FT37; -.
DR SMR; Q9FT37; -.
DR BioCyc; MetaCyc:MON-14814; -.
DR BRENDA; 4.2.3.17; 9720.
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 2: Evidence at transcript level;
KW Lyase; Magnesium; Metal-binding; Taxol biosynthesis.
FT CHAIN 1..862
FT /note="Taxadiene synthase"
FT /id="PRO_0000186451"
FT REGION 45..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 98070 MW; 3A597BAF722BF679 CRC64;
MAQLSFNAAL KMNALGNKAI HDPTNCRAKS EGQMMWVCSK SGRTRVKMSR GSGGPGPVVM
MSSSTGTSKV VSETSSTIVD DIPRLSANYH GDLWHHNVIQ TLETPFRESS TYQERADELV
VKIKDMFNAL GDGDISPSAY DTAWVARVAT ISSDGSEKPR FPQALNWVFN NQLQDGSWGI
ESHFSLCDRL LNTTNSVIAL SVWKTGHSQV EQGTEFIAEN LRLLNEEDEL SPDFEIIFPA
LLQKAKALGI NLPYDLPFIK YLSTTREARL TDVSAAADNI PANMLNALEG LEEVMDWKKI
MRFQSKDGSF LSSPASTACV LMNTGDEKCF TFLNNLLVKF GGCVPCMYSI DLLERLSLVD
NIEHLGIGRH FKQEIKVALD YVYRHWSERG IGWGRDSLVP DLNTTALGLR TLRTHGYDVS
SDVLNNFKDE NGRFFSSAGQ THVELRSVVI LFRASDLAFP DEGAMDDARK FAEPYLRDAL
ATKISTNTKL FKEIEYVVEY PWHMSIPRSE ARSYIDSYDD DYVWERKTLY RMPSLSNSKC
LELAKLDFNI VQSLHQEELK LLTRWWKESG MADINFTRHR VAEVYFSSAT FEPEYSATRI
AFTKIGCLQV LFDDMADIFA TLDELKSFTE GVKRWDTSLL HEIPECMQTC FKVWFKLIEE
VNNDVVKVQG RDMLAHIRKP WELYFNCYVQ EREWLDAGYI PTFEEYLKTY AISVGLGPCT
LQPILLMGEL VKDDVVEKVH YPSNMFELVS LSWRLTNDTK TYQAEKARGQ QASGIACYMK
DNLGATEEDA IKHICRVVDR ALKEASFEYF KPSNDIPMGC KSFIFNLRLC VQIFYKFIDG
YGIANEEIKD YIRKVYIDPI QV
