TPSD2_PICAB
ID TPSD2_PICAB Reviewed; 867 AA.
AC Q675L5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Bifunctional isopimaradiene synthase, chloroplastic;
DE AltName: Full=Diterpene synthase;
DE AltName: Full=PaTPS-Iso;
DE Includes:
DE RecName: Full=Isopimara-7,15-diene synthase;
DE Short=Isopimaradiene synthase;
DE EC=4.2.3.44;
DE Includes:
DE RecName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12;
DE Flags: Precursor;
GN Name=TPS-ISO;
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, CATALYTIC ACTIVITY, GENE FAMILY, AND
RP 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).
RN [2]
RP SEQUENCE REVISION.
RA Martin D.M., Keeling C., Bohlmann J.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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 isopimara-7,15-diene. {ECO:0000250,
CC 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 Evidence={ECO:0000269|PubMed:15310829};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + isopimara-7,15-diene;
CC Xref=Rhea:RHEA:26128, ChEBI:CHEBI:33019, ChEBI:CHEBI:52280,
CC ChEBI:CHEBI:58635; EC=4.2.3.44;
CC Evidence={ECO:0000269|PubMed:15310829};
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}.
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DR EMBL; AY473620; AAS47690.2; -; mRNA.
DR AlphaFoldDB; Q675L5; -.
DR SMR; Q675L5; -.
DR KEGG; ag:AAS47690; -.
DR BioCyc; MetaCyc:MON-12744; -.
DR BRENDA; 4.2.3.35; 4815.
DR BRENDA; 4.2.3.44; 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: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..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..867
FT /note="Bifunctional isopimaradiene synthase, chloroplastic"
FT /id="PRO_0000348953"
FT MOTIF 400..403
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 619..623
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 400
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 402
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 487
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 619
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 619
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 623
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 623
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 BINDING 767
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 771
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 867 AA; 99203 MW; 7E27A5BBCC6062D7 CRC64;
MALLSSSLSS QIPTGSHPLT HTQCIPHFST TINAGISAGK PRSFYLRWGK GSNKIIACVG
EGTTSLPYQS AEKTDSLSAP TLVKREFPPG FWKDHVIDSL TSSHKVSAAE EKRMETLISE
IKNIFRSMGY GETNPSAYDT AWVARIPAVD GSEHPEFPET LEWILQNQLK DGSWGEGFYF
LAYDRILATL ACIITLTLWR TGETQIRKGI EFFKTQAGKI EDEADSHRPS GFEIVFPAML
KEAKVLGLDL PYELPFIKQI IEKREAKLER LPTNILYALP TTLLYSLEGL QEIVDWEKII
KLQSKDGSFL TSPASTAAVF MRTGNKKCLE FLNFVLKKFG NHVPCHYPLD LFERLWAVDT
VERLGIDHHF KEEIKDALDY VYSHWDERGI GWARENPIPD IDDTAMGLRI LRLHGYNVSS
DVLKTFRDEN GEFFCFLGQT QRGVTDMLNV NRCSHVAFPG ETIMQEAKLC TERYLRNALE
DVGAFDKWAL KKNIRGEVEY ALKYPWHRSM PRLEARSYIE HYGPNDVWLG KTMYMMPYIS
NLKYLELAKL DFNHVQSLHQ KELRDLRRWW KSSGLSELKF TRERVTEIYF SAASFIFEPE
FATCRDVYTK ISIFTVILDD LYDAHGTLDN LELFSEGVKR WDLSLVDRMP QDMKICFTVL
YNTVNEIAVE GRKRQGRDVL GYIRNVLEIL LAAHTKEAEW SAARYVPSFD EYIENASVSI
SLGTLVLISV LFTGEILTDD VLSKIGRGSR FLQLMGLTGR LVNDTKTYEA ERGQGEVASA
VQCYMKEHPE ISEEEALKHV YTVMENALDE LNREFVNNRD VPDSCRRLVF ETARIMQLFY
MEGDGLTLSH EMEIKEHVKN CLFQPVA
