LEVOS_PICSI
ID LEVOS_PICSI Reviewed; 859 AA.
AC F2XFB2; Q20HU9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Bifunctional levopimaradiene synthase, chloroplastic {ECO:0000303|PubMed:21385377};
DE AltName: Full=Abietadiene synthase {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.18 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Levopimaradiene synthase;
DE EC=4.2.3.32 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-LAS {ECO:0000303|PubMed:21385377};
DE Short=PsTPS-LAS {ECO:0000303|PubMed:21385377};
DE Short=PsTPS-LASl {ECO:0000303|PubMed:16415217};
DE Flags: Precursor;
GN Name=TPS-LAS {ECO:0000303|PubMed:16415217, ECO:0000303|PubMed:21385377};
GN Synonyms=TPS-LASl {ECO:0000303|PubMed:16415217};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, FUNCTION,
RP PATHWAY, AND GENE FAMILY.
RC STRAIN=cv. FB3-425;
RX PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA Dullat H.K., Bohlmann J.;
RT "Transcriptome mining, functional characterization, and phylogeny of a
RT large terpene synthase gene family in spruce (Picea spp.).";
RL BMC Plant Biol. 11:43-43(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-627 (ISOFORM 2), AND INDUCTION BY WOUNDING.
RX PubMed=16415217; DOI=10.1104/pp.105.071803;
RA Byun-McKay A., Godard K.-A., Toudefallah M., Martin D.M., Alfaro R.,
RA King J., Bohlmann J., Plant A.L.;
RT "Wound-induced terpene synthase gene expression in Sitka spruce that
RT exhibit resistance or susceptibility to attack by the white pine weevil.";
RL Plant Physiol. 140:1009-1021(2006).
CC -!- FUNCTION: Terpene synthase (di-TPS) involved in the biosynthesis of
CC diterpene natural products included in conifer oleoresin secretions and
CC volatile emissions; these compounds contribute to biotic and abiotic
CC stress defense against herbivores and pathogens (PubMed:21385377).
CC Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to
CC isopimaradiene (PubMed:21385377). {ECO:0000269|PubMed:21385377}.
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:21385377};
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:21385377};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:16415217}.
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F2XFB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F2XFB2-2; Sequence=VSP_061467, VSP_061468;
CC -!- INDUCTION: Accumulates in apical leaders upon wounding in both
CC resistant and susceptible to white pine weevil (Pissodes strobi)
CC plants. {ECO:0000269|PubMed:16415217}.
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; HQ426170; ADZ45517.1; -; mRNA.
DR EMBL; DQ195273; ABA86246.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050554; F:abietadiene synthase activity; IDA:UniProtKB.
DR GO; GO:0052678; F:levopimaradiene synthase activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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 Alternative splicing; Chloroplast; Lyase; Magnesium; Metal-binding;
KW Plastid; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..859
FT /note="Bifunctional levopimaradiene synthase,
FT chloroplastic"
FT /id="PRO_0000454419"
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 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 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 763
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT VAR_SEQ 55
FT /note="K -> KDNQAKKL (in isoform 2)"
FT /id="VSP_061467"
FT VAR_SEQ 156..160
FT /note="ILQNQ -> FFKIS (in isoform 2)"
FT /id="VSP_061468"
FT CONFLICT 192
FT /note="R -> Q (in Ref. 2; ABA86246)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="T -> S (in Ref. 2; ABA86246)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="V -> I (in Ref. 2; ABA86246)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="L -> P (in Ref. 2; ABA86246)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="N -> I (in Ref. 2; ABA86246)"
FT /evidence="ECO:0000305"
FT CONFLICT 623..627
FT /note="LKLFS -> SVVSD (in Ref. 2; ABA86246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 98563 MW; 51734C24C4A60DF7 CRC64;
MALLSSSLSS HIPTGAHHLT LNAYANTQCI PHFFSTLNAG TSAGKRSSLY LRWGKGSNKI
IACVGEDSVS APTLLKREFP PGFWKDHVID SLTSSHKVAA SDEKRIETLI SEIKNMFRSM
GYGETNPSAY DTAWVARIPA VDGSEQPEFP ETLEWILQNQ LKDGSWGEGF YFLAYDRILA
TLACIITLTL WRTGEIQVQK GIEFFKTQAV KIEDEADSHR PSGFEIVFPA MLKEAKVLGL
DLPYELPFIK KIIEKREAKL ERLPTNILYA LPTTLLYSLE GLQEIVDWQK IIKLQSKDGS
FLTSPASTAA VFMRTGNKKC LEFLNFVLKK FGNHVPCHYP LDLFERLWAV DTVERLGIDR
HFKEEIKDAL DYVYSHWDER GIGWARENLV 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 MPEDMKICFM GFYNTFNEIA
EEGRKRQGRD VLGYIRNVWE IQLEAYTKEA EWSAARYVPS FDEYIENASV SIALGTVVLI
SALFTGEILT DDVLSKIGRG SRFLQLMGLT GRLVNDTKTY EAERGQGEVA SAVQCYMKDH
PEISEEEALK HVYTVMENAL DELNREFVNN REVPDSCRRL VFETARIMQL FYMDGDGLTL
SHETEIKEHV KNCLFHPVA
