TPSD2_PINCO
ID TPSD2_PINCO Reviewed; 850 AA.
AC M4HYC6;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Bifunctional levopimaradiene synthase, chloroplastic {ECO:0000303|PubMed:23370714};
DE Short=PcLAS2 {ECO:0000303|PubMed:23370714};
DE AltName: Full=Diterpene synthase;
DE Includes:
DE RecName: Full=Levopimaradiene synthase;
DE EC=4.2.3.32 {ECO:0000269|PubMed:23370714};
DE AltName: Full=Abieta-7,13-diene synthase;
DE EC=4.2.3.18 {ECO:0000269|PubMed:23370714};
DE AltName: Full=Neoabietadiene synthase;
DE EC=4.2.3.132 {ECO:0000269|PubMed:23370714};
DE Includes:
DE RecName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12 {ECO:0000269|PubMed:23370714};
DE Flags: Precursor;
GN Name=TPS-LAS2 {ECO:0000303|PubMed:23370714};
OS Pinus contorta (Shore pine) (Lodgepole pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3339 {ECO:0000312|EMBL:AFU73863.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23370714; DOI=10.1104/pp.112.208546;
RA Hall D.E., Zerbe P., Jancsik S., Quesada A.L., Dullat H., Madilao L.L.,
RA Yuen M., Bohlmann J.;
RT "Evolution of conifer diterpene synthases: diterpene resin acid
RT biosynthesis in lodgepole pine and jack pine involves monofunctional and
RT bifunctional diterpene synthases.";
RL Plant Physiol. 161:600-616(2013).
CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC response to insect attack or other injury. Involved in diterpene (C20)
CC olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential
CC cyclizations of geranylgeranyl diphosphate (GGPP) to levopimaradiene.
CC Levopimaradiene is the major products of the enzyme with abietadiene
CC and neoabietadiene. No activity with farnesyl diphosphate (FPP) as
CC substrate. {ECO:0000269|PubMed:23370714}.
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 Evidence={ECO:0000269|PubMed:23370714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate;
CC Xref=Rhea:RHEA:13873, ChEBI:CHEBI:30232, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.18;
CC Evidence={ECO:0000269|PubMed:23370714};
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 Evidence={ECO:0000269|PubMed:23370714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + neoabietadiene;
CC Xref=Rhea:RHEA:33987, ChEBI:CHEBI:29651, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.132;
CC Evidence={ECO:0000269|PubMed:23370714};
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 -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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; JQ240311; AFU73863.1; -; mRNA.
DR AlphaFoldDB; M4HYC6; -.
DR SMR; M4HYC6; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050554; F:abietadiene synthase activity; IEA:UniProtKB-EC.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; Plant defense; Plastid; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..850
FT /note="Bifunctional levopimaradiene synthase,
FT chloroplastic"
FT /id="PRO_0000431417"
FT MOTIF 383..386
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 602..606
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 602
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 602
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 606
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 606
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 754
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 850 AA; 97780 MW; 560E98826F636CE1 CRC64;
MALPSSSLSS QIHTGATTQC IPHFHGSLNA GTSAGKRRSL YLRWGKGPSK IVACAGQDPF
SVPTLVKREF PPGFWKDHVI ESLMPSYKVA PSDEKRIETL ITEIKNMFRS MGYGETNPSA
YDTAWVARIP AVDGSEKPQF PETLEWILQN QLKDGSWGEE FYFLAYDRIL ATLACIITLT
IWQTGDTQVQ KGIEFFKTQA GKIEEEADSH RPSGFEIVFP AMLKEAKALG LALPYELPFI
QQIIEKREAK LQRLPSDLLY ALPTTLLYSL EGLQEIVDWE KIMKLQSKDR SFLSSPSSTA
AVFMRTGNKK CLEFLNFVLK KFGNHVPCHY PLDLFERLWA VDTVERLGID HHFKEEIKDA
LDYVYSHWDE RGIGWARENP VPDIDDTAMG LRILRLHGYN VSSDVLKTFR DENGEFFCFL
GQTQRGVTDM LNVNRCSHVA FPGETIMEEA KLCTERYLRN ALEDTGAFDK WALKKNIRGE
VEYALKYPWH RSMPRLEARS YIENYGPNDV WLGKTMYMMP NISNEKYLEL AKLDFNRVQF
FHRQELQDIR RWWNSSGFSQ LGFTRERVAE IYFSPASFLF EPEFATCRAV YTKTSNFTVI
LDDLYDAHGT LDNLKLFSES VKRWDLSLVD QMPQDMKICF KGFYNTFNEI AEEGRKRQGR
DVLSYIQKVW EVQLEAYTKE AEWSAVRYVP SYDEYIENAS VSIALGTVVL ISALFTGEIL
TDDILSKIGR DSRFLYLMGL TGRLVNDTKT YQAERGQGEV ASAVQCYMKD HPEISEEEAL
KHVYTIMDNA LDELNREFVN NRDVPDTCRR LVFETARIMQ LFYMDGDGLT LSHNMEIKEH
VKNCLFQPVA
