TPSD1_PICAB
ID TPSD1_PICAB Reviewed; 859 AA.
AC Q675L4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Bifunctional levopimaradiene synthase, chloroplastic;
DE AltName: Full=Diterpene synthase;
DE AltName: Full=PaTPS-LAS;
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=TPS-LAS;
OS Picea abies (Norway spruce) (Picea excelsa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, 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).
CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC response to insect attack or other injury (By similarity). Involved in
CC diterpene (C20) olefins biosynthesis. Bifunctional enzyme that
CC catalyzes two sequential cyclizations of geranylgeranyl diphosphate
CC (GGPP) to levopimaradiene. Levopimaradiene is the major products of the
CC enzyme followed by abietadiene, neoabietadiene and palustradiene.
CC {ECO:0000250, ECO:0000269|PubMed:15310829}.
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 -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY473621; AAS47691.1; -; mRNA.
DR AlphaFoldDB; Q675L4; -.
DR SMR; Q675L4; -.
DR BioCyc; MetaCyc:MON-12742; -.
DR BRENDA; 4.2.3.18; 4815.
DR BRENDA; 4.2.3.32; 4815.
DR BRENDA; 5.5.1.12; 4815.
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: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 2: Evidence at transcript level;
KW Chloroplast; Isomerase; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Plant defense; Plastid; Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..859
FT /note="Bifunctional levopimaradiene synthase,
FT chloroplastic"
FT /id="PRO_0000348952"
FT MOTIF 392..395
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 611..615
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
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 394
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 755
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 759
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 763
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 859 AA; 98458 MW; BD98408794AC8CAB CRC64;
MALLSSSLSS QIPTGAHHLT LNAYANTQCI PHFFSTLNAG TSAGKRSSLY LRWGKGSNKI
IACVGEDSLS APTLVKREFP PGFWKDHVID SLTSSHKVAA SDEKRIETLI SEIKNMFRSM
GYGDTNPSAY DTAWVARIPA VDGSEQPEFP ETLEWILQNQ LKDGSWGEGF YFLAYDRILA
TLACIITLTL WRTGEIQVQK GIEFFKTQAG KIEDEADSHR PSGFEIVFPA MLKEAKVLGL
DLPYELPFIK QIIEKREAKL ERLPTNILYA LPTTLLYSLE GLQEIVDWQK IIKLQSKDGS
FLSSPASTAA VFMRTGNKKC LEFLNFVLKK FGNHVPCHYP LDLFERLWAV DTIERLGIDR
HFKEEIKDAL DYVYSHWDER GIGWARENPV PDIDDTAMGL RILRLHGYNV SSDVLKTFRD
ENGEFFCFLG QTQRGVTDML NVNRCSHVAF PGETIMEEAK TCTERYLRNA LEDVGAFDKW
ALKKNIRGEV EYALKYPWHR SMPRLEARSY IEHYGPNDVW LGKTMYMMPY ISNEKYLELA
KLDFNHVQSL HQKELRDLRR WWTSSGFTEL KFTRERVTEI YFSPASFMFE PEFATCRAVY
TKTSNFTVIL DDLYDAHGTL DDLKLFSDSV KKWDLSLVDR MPQDMKICFM GFYNTFNEIA
EEGRKRQGRD VLGYIRNVWE IQLEAYTKEA EWSAARYVPS FDEYIDNASV SIALGTVVLI
SALFTGEILT DDVLSKIGRG SRFLQLMGLT GRLVNDTKTY EAERGQGEVA SAVQCYMKDH
PEISEEEALK HVYTVMENAL DELNREFVNN REVPDSCRRL VFETARIMQL FYMDGDGLTL
SHETEIKEHV KNCLFQPVA
