TPSD1_GINBI
ID TPSD1_GINBI Reviewed; 873 AA.
AC Q947C4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Bifunctional levopimaradiene synthase, chloroplastic;
DE AltName: Full=Diterpene synthase;
DE AltName: Full=GbTPS-Lev;
DE Includes:
DE RecName: Full=Levopimaradiene synthase;
DE EC=4.2.3.32;
DE Includes:
DE RecName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12;
DE Flags: Precursor;
GN Name=LPS;
OS Ginkgo biloba (Ginkgo) (Maidenhair tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Ginkgoidae; Ginkgoales; Ginkgoaceae; Ginkgo.
OX NCBI_TaxID=3311;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=11488601; DOI=10.1006/abbi.2001.2438;
RA Schepmann H.G., Pang J., Matsuda S.P.;
RT "Cloning and characterization of Ginkgo biloba levopimaradiene synthase
RT which catalyzes the first committed step in ginkgolide biosynthesis.";
RL Arch. Biochem. Biophys. 392:263-269(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lee K.I., Chang Y.J., Kim S.U.;
RT "Genomic structure of levopimaradiene synthase from Ginkgo biloba.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15310829; DOI=10.1104/pp.104.042028;
RA Martin D.M., Faeldt J., Bohlmann J.;
RT "Functional characterization of nine Norway Spruce TPS genes and evolution
RT of gymnosperm terpene synthases of the TPS-d subfamily.";
RL Plant Physiol. 135:1908-1927(2004).
RN [4]
RP FUNCTION.
RX PubMed=16497345; DOI=10.1016/j.phytochem.2006.01.011;
RA Ro D.-K., Bohlmann J.;
RT "Diterpene resin acid biosynthesis in loblolly pine (Pinus taeda):
RT functional characterization of abietadiene/levopimaradiene synthase (PtTPS-
RT LAS) cDNA and subcellular targeting of PtTPS-LAS and
RT abietadienol/abietadienal oxidase (PtAO, CYP720B1).";
RL Phytochemistry 67:1572-1578(2006).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16534728; DOI=10.1055/s-2005-916180;
RA Kim S.M., Kuzuyama T., Chang Y.J., Song K.S., Kim S.U.;
RT "Identification of class 2 1-deoxy-D-xylulose 5-phosphate synthase and 1-
RT deoxy-D-xylulose 5-phosphate reductoisomerase genes from Ginkgo biloba and
RT their transcription in embryo culture with respect to ginkgolide
RT biosynthesis.";
RL Planta Med. 72:234-240(2006).
CC -!- FUNCTION: Catalyzes the initial cyclization step in the biosynthesis of
CC ginkgolides, a structurally unique family of diterpenoids that are
CC highly specific platelet-activating-factor receptor antagonists.
CC Bifunctional enzyme that catalyzes two sequential cyclizations of
CC geranylgeranyl diphosphate (GGPP) to levopimaradiene.
CC {ECO:0000269|PubMed:16497345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:58756; EC=5.5.1.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate;
CC Xref=Rhea:RHEA:25548, ChEBI:CHEBI:29616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.32;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2.;
CC -!- PATHWAY: Terpene metabolism; ginkgolide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:16534728}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity in the class II active site relevant for the cyclization of
CC GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the
CC catalytic activity in the class I active site, presumably through
CC binding to Mg(2+). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; AF331704; AAL09965.1; -; mRNA.
DR EMBL; AY574248; AAS89668.1; -; Genomic_DNA.
DR AlphaFoldDB; Q947C4; -.
DR SMR; Q947C4; -.
DR KEGG; ag:AAL09965; -.
DR BRENDA; 4.2.3.32; 2435.
DR UniPathway; UPA00961; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0052678; F:levopimaradiene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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 Chloroplast; Isomerase; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Plastid; Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..873
FT /note="Bifunctional levopimaradiene synthase,
FT chloroplastic"
FT /id="PRO_0000348950"
FT MOTIF 405..408
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 624..628
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 407
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 624
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 624
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 628
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 628
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 769
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 777
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 873 AA; 100290 MW; F2C980BB19F9931E CRC64;
MAGVLFANLP CSLQLSPKVP FRQSTNILIP FHKRSSFGFN AQHCVRSHLR LRWNCVGIHA
SAAETRPDQL PQEERFVSRL NADYHPAVWK DDFIDSLTSP NSHATSKSSV DETINKRIQT
LVKEIQCMFQ SMGDGETNPS AYDTAWVARI PSIDGSGAPQ FPQTLQWILN NQLPDGSWGE
ECIFLAYDRV LNTLACLLTL KIWNKGDIQV QKGVEFVRKH MEEMKDEADN HRPSGFEVVF
PAMLDEAKSL GLDLPYHLPF ISQIHQKRQK KLQKIPLNVL HNHQTALLYS LEGLQDVVDW
QEITNLQSRD GSFLSSPAST ACVFMHTQNK RCLHFLNFVL SKFGDYVPCH YPLDLFERLW
AVDTVERLGI DRYFKKEIKE SLDYVYRYWD AERGVGWARC NPIPDVDDTA MGLRILRLHG
YNVSSDVLEN FRDEKGDFFC FAGQTQIGVT DNLNLYRCSQ VCFPGEKIME EAKTFTTNHL
QNALAKNNAF DKWAVKKDLP GEVEYAIKYP WHRSMPRLEA RSYIEQFGSN DVWLGKTVYK
MLYVSNEKYL ELAKLDFNMV QALHQKETQH IVSWWRESGF NDLTFTRQRP VEMYFSVAVS
MFEPEFAACR IAYAKTSCLA VILDDLYDTH GSLDDLKLFS EAVRRWDISV LDSVRDNQLK
VCFLGLYNTV NGFGKDGLKE QGRDVLGYLR KVWEGLLASY TKEAEWSAAK YVPTFNEYVE
NAKVSIALAT VVLNSIFFTG ELLPDYILQQ VDLRSKFLHL VSLTGRLIND TKTYQAERNR
GELVSSVQCY MRENPECTEE EALSHVYGII DNALKELNWE LANPASNAPL CVRRLLFNTA
RVMQLFYMYR DGFGISDKEM KDHVSRTLFD PVA
