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 13-SEP-2023, entry version 82. 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}. 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; AY473620; AAS47690.2; -; mRNA. DR AlphaFoldDB; Q675L5; -. DR SMR; Q675L5; -. DR KEGG; ag:AAS47690; -. DR BioCyc; MetaCyc:MONOMER-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; 1.50.10.160; -; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 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 PANTHER; PTHR31739; ENT-COPALYL DIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR31739:SF4; ENT-COPALYL DIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1. DR SFLD; SFLDG01014; Terpene_Cyclase_Like_1_N-term; 1. DR SFLD; SFLDG01605; Terpene_Cyclase_Like_1_N-term; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 2. DR SUPFAM; SSF48576; Terpenoid synthases; 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 //