TASY_TAXBR
ID TASY_TAXBR Reviewed; 862 AA.
AC Q41594; Q94FV8;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 brevifolia (Pacific yew).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Taxaceae;
OC Taxus.
OX NCBI_TaxID=46220;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8621577; DOI=10.1074/jbc.271.16.9201;
RA Wildung M.R., Croteau R.B.;
RT "A cDNA clone for taxadiene synthase, the diterpene cyclase that catalyzes
RT the committed step of taxol biosynthesis.";
RL J. Biol. Chem. 271:9201-9204(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11404343; DOI=10.1093/genetics/158.2.811;
RA Trapp S.C., Croteau R.B.;
RT "Genomic organization of plant terpene synthases and molecular evolutionary
RT implications.";
RL Genetics 158:811-832(2001).
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; U48796; AAC49310.1; -; mRNA.
DR EMBL; AF326519; AAK83566.1; -; Genomic_DNA.
DR PDB; 3P5P; X-ray; 1.82 A; A=108-862.
DR PDB; 3P5R; X-ray; 2.25 A; A/B=108-862.
DR PDBsum; 3P5P; -.
DR PDBsum; 3P5R; -.
DR AlphaFoldDB; Q41594; -.
DR SMR; Q41594; -.
DR KEGG; ag:AAC49310; -.
DR BioCyc; MetaCyc:MON-13385; -.
DR BRENDA; 4.2.3.17; 6223.
DR UniPathway; UPA00842; UER00806.
DR EvolutionaryTrace; Q41594; -.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Metal-binding; Taxol biosynthesis.
FT CHAIN 1..862
FT /note="Taxadiene synthase"
FT /id="PRO_0000186450"
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"
FT CONFLICT 148
FT /note="L -> V (in Ref. 2; AAK83566)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="A -> V (in Ref. 2; AAK83566)"
FT /evidence="ECO:0000305"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3P5R"
FT HELIX 186..202
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 207..221
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3P5R"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 351..365
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 445..455
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 463..482
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 489..499
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 507..517
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:3P5P"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 538..568
FT /evidence="ECO:0007829|PDB:3P5P"
FT TURN 571..575
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 578..587
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 596..618
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 622..634
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 645..669
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 674..696
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 703..713
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 716..725
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 744..766
FT /evidence="ECO:0007829|PDB:3P5P"
FT TURN 767..769
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 774..781
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 787..810
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 818..826
FT /evidence="ECO:0007829|PDB:3P5P"
FT HELIX 828..834
FT /evidence="ECO:0007829|PDB:3P5P"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:3P5R"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:3P5R"
FT HELIX 848..856
FT /evidence="ECO:0007829|PDB:3P5P"
SQ SEQUENCE 862 AA; 98304 MW; 9141B59780CD79A1 CRC64;
MAQLSFNAAL KMNALGNKAI HDPTNCRAKS ERQMMWVCSR SGRTRVKMSR GSGGPGPVVM
MSSSTGTSKV VSETSSTIVD DIPRLSANYH GDLWHHNVIQ TLETPFRESS TYQERADELV
VKIKDMFNAL GDGDISPSAY DTAWVARLAT ISSDGSEKPR FPQALNWVFN NQLQDGSWGI
ESHFSLCDRL LNTTNSVIAL SVWKTGHSQV QQGAEFIAEN LRLLNEEDEL SPDFQIIFPA
LLQKAKALGI NLPYDLPFIK YLSTTREARL TDVSAAADNI PANMLNALEG LEEVIDWNKI
MRFQSKDGSF LSSPASTACV LMNTGDEKCF TFLNNLLDKF GGCVPCMYSI DLLERLSLVD
NIEHLGIGRH FKQEIKGALD YVYRHWSERG IGWGRDSLVP DLNTTALGLR TLRMHGYNVS
SDVLNNFKDE NGRFFSSAGQ THVELRSVVN LFRASDLAFP DERAMDDARK FAEPYLREAL
ATKISTNTKL FKEIEYVVEY PWHMSIPRLE ARSYIDSYDD NYVWQRKTLY 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
