TPSD1_PINBN
ID TPSD1_PINBN Reviewed; 857 AA.
AC M4HXU6;
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=PbLAS1 {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-LAS1 {ECO:0000303|PubMed:23370714};
OS Pinus banksiana (Jack pine) (Pinus divaricata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3353 {ECO:0000312|EMBL:AFU73864.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND 3D-STRUCTURE
RP MODELING.
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; JQ240312; AFU73864.1; -; mRNA.
DR AlphaFoldDB; M4HXU6; -.
DR SMR; M4HXU6; -.
DR BRENDA; 5.5.1.12; 4842.
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..33
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 34..857
FT /note="Bifunctional levopimaradiene synthase,
FT chloroplastic"
FT /id="PRO_0000431418"
FT MOTIF 390..393
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 609..613
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 390
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 609
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 609
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 613
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 613
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 757
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 761
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 857 AA; 98479 MW; C52B65619C9E932E CRC64;
MALPSSSLSS QIHTGATTQC IPHFHGSLNA GTSAGKRRSL YLRWGKDNQA KKFGPSKIVA
CAGQDPFSVP TLVKREFPPG FWKDHVIESL MPSYKVAPSD EKRIETLITE IKNMFRSMGY
GETNPSAYDT AWVARIPAVD GSEKPQFPET LEWILQNQLK DGSWGEEFYF LAYDRILATL
ACIITLTIWQ TGDTQVQKGI EFFKTQAGKI EEEADSHRPS GFEIVFPAML KEAKALGLDL
PYELPFIQQI IEKREAKLQR LPPDLLYALP TTLLYSLEGL QEIVDWEKIM KLQSKDGSFL
SSPASTAAVF MRTGNKKCLE FLNFVLKKFG NHVPCHYPLD LFERLWAVDT VERLGIDHHF
KEEIKDALDY VYSHWDERGI GWARENPVPD IDDTAMGLRI LRLHGYNVSS DVLKTFRDEN
GEFFCFLGQT QRGVTDMLNV NRCSHVAFPG ETIMEEAKLC TERYLRNALE DTGAFDKWAL
KKNIRGEVEY ALKYPWHRSM PRLEARSYIE NYGPNDVWLG KTMYMMPNIS NEKYLELAKL
DFNRVQFFHR QELQDIRRWW NSSGFSQLGF TRERVAEIYF SPASFLFEPE FATCRAVYTK
TSNFTVILDD LYDAHGTLDN LKLFSESVKR WDLSLVDQMP QDMKICFKGF YNTFNEIAEE
GRKRQGRDVL SYIQKVWEVQ LEAYTKEAEW SAVRYVPSYD EYIGNASVSI ALGTVVLISA
LFTGEILTDD ILSKIGRDSR FLYLMGLTGR LVNDTKTYQA ERGQGEVASA VQCYMKDHPE
ISEEEALKHV YTIMDNALDE LNREFVNNRD VPDTCRRLVF ETARIMQLFY MDGDGLTLSH
NMEIKEHVKN CLFQPVA
