TPSD1_PINTA
ID TPSD1_PINTA Reviewed; 850 AA.
AC Q50EK2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Bifunctional levopimaradiene synthase, chloroplastic;
DE Short=PtLAS;
DE AltName: Full=Diterpene synthase;
DE AltName: Full=PtTPS-LAS;
DE Includes:
DE RecName: Full=Levopimaradiene synthase;
DE EC=4.2.3.32;
DE AltName: Full=Neoabietadiene synthase;
DE EC=4.2.3.132;
DE Includes:
DE RecName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12;
DE Flags: Precursor;
GN Name=LPS;
OS Pinus taeda (Loblolly pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3352;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15911762; DOI=10.1073/pnas.0500825102;
RA Ro D.-K., Arimura G., Lau S.Y.W., Piers E., Bohlmann J.;
RT "Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a
RT multifunctional, multisubstrate cytochrome P450 monooxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8060-8065(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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).
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 followed by
CC abietadiene, neoabietadiene and palustradiene. No activity with geranyl
CC diphosphate (GPP) or farnesyl diphosphate (FPP) as substrate.
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 Evidence={ECO:0000269|PubMed:16497345};
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:16497345};
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:16497345};
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.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16497345}.
CC -!- TISSUE SPECIFICITY: Expressed in young tissues such as flushing buds
CC and green bark tissues. Lower levels in mature needles and bark.
CC {ECO:0000269|PubMed:15911762}.
CC -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:15911762}.
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; AY779541; AAX07435.1; -; mRNA.
DR AlphaFoldDB; Q50EK2; -.
DR SMR; Q50EK2; -.
DR KEGG; ag:AAX07435; -.
DR BioCyc; MetaCyc:MON-12741; -.
DR BRENDA; 4.2.3.18; 4861.
DR BRENDA; 4.2.3.32; 4861.
DR UniPathway; UPA00924; -.
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..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..850
FT /note="Bifunctional levopimaradiene synthase,
FT chloroplastic"
FT /id="PRO_0000348951"
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; 97499 MW; 20A7EC6BFA29207F 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 LQRLPPDLLY ALPTTLLYSL EGLQEIVDWE KIMKLQSKDG SFLSSPASTA
AVFMRTGNKK CLEFLNFVLK KFGNHVPCHY PLDLFERLWA VDTVERLGID HHFKEEIKDA
LDYVYSHWDE RGIGWARENP VPDIDDTAMG LRILRLHGYN VSSDVLKTFR DENGEFFCFL
GQTQRGVTDM LNVNRCSHVA FPGETIMEEA KLCTERYLRN ALEDGGASDK WALKKNIRGE
VEYALKYPWH RSMPRLEARS YIENYGPNDV WLGKTMYMMP NISNEKYLEL AKLDFNRVQF
FHRQELQDIR RWWNSSGFSQ LGFTRERVAE IYFSPASFLF EPEFATCRAV YTKTSNFTVI
LDDLYDAHGT LDNLKLFSES VKRWDLSLVD QMPQDMKICF KGFYNTFNEI AEEGRKRQGR
DVLSYIQKVW EVQLEAYTKE AEWSAVRYVP SYDEYIGNAS VSIALGTVVL ISALFTGEIL
TDDILSKIGR DSRFLYLMGL TGRLVNDTKT YQAERGQGEV ASAVQCYMKD HPEISEEEAL
KHVYTIMDNA LDELNREFVN NRDVPDTCRR LVFETARIMQ LFYMDGDGLT LSHNMEIKEH
VKNCLFQPVA
