3CAR2_PINBN
ID 3CAR2_PINBN Reviewed; 626 AA.
AC R9QMR6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=(+)-3-carene synthase 2, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.107 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Terpene synthase (+)3car2 {ECO:0000303|PubMed:23679205};
DE Short=PbTPS-(+)3car2 {ECO:0000303|PubMed:23679205};
DE Flags: Precursor;
GN Name=TPS-(+)3car2 {ECO:0000303|PubMed:23679205};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23679205; DOI=10.1186/1471-2229-13-80;
RA Hall D.E., Yuen M.M.S., Jancsik S., Quesada A.L., Dullat H.K., Li M.,
RA Henderson H., Arango-Velez A., Liao N.Y., Docking R.T., Chan S.K.,
RA Cooke J.E.K., Breuil C., Jones S.J.M., Keeling C.I., Bohlmann J.;
RT "Transcriptome resources and functional characterization of monoterpene
RT synthases for two host species of the mountain pine beetle, lodgepole pine
RT (Pinus contorta) and jack pine (Pinus banksiana).";
RL BMC Plant Biol. 13:80-80(2013).
CC -!- FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of
CC monoterpene natural products included in conifer oleoresin secretions
CC and volatile emissions; these compounds contribute to biotic and
CC abiotic stress defense against herbivores and pathogens
CC (PubMed:23679205). Catalyzes the conversion of (2E)-geranyl diphosphate
CC (GPP) to (+)-3-carene (PubMed:23679205). {ECO:0000269|PubMed:23679205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (+)-car-3-ene + diphosphate;
CC Xref=Rhea:RHEA:32539, ChEBI:CHEBI:7, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.107;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32540;
CC Evidence={ECO:0000269|PubMed:23679205};
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 Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:23679205}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:23679205}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; JQ240306; AFU73858.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA: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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..626
FT /note="(+)-3-carene synthase 2, chloroplastic"
FT /id="PRO_0000455012"
FT MOTIF 377..381
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 626 AA; 71417 MW; C784332BAEFF4977 CRC64;
MSLISAVPLA SSCVSKSLIS SVREHTALRR AIATLQMSRR GKSVAASIRM SSATAGSDDG
VKRRIGDYHS NLWDDNFIQS LSSPYGASSY GEHADRLIGE VKEIFNSFSI ADGELISPVN
DLLQQLWMVD NVERLGIDRH FQTEIKVALD YVYRYWSEEG IGCGRDSAFT DLNTTALAFR
IFRLHGYTVS SDVFEHFKDQ KGQFAASAND TELQTRSVFN LFRASLIAFP EEKVLEEAEK
FAAAYLKAAL QTLPVSGLSR EIQYVFDYRW HSNLPRLEAR SYIDILADNT ISGTPDANTK
KLLELAKLEF NIFHSVQQKE LQCLWRWWKE WGCPELTFIR HRYVEFYTLV SGIDMVPEHA
TFRLSCVKTC HLITILDDMY DTFGTIDELR LFTAAVKRWD PSATECLPEY MKGVYMVLYE
TVNEMAKEAQ KSQRRDTLGY VRQALEDYIG SYLKEAEWIA TGYVPTFQEY FENGKLSSGH
RIATLQPILT LSIPFPHHIL QEIDFPSKFN DYAASILRLR GDTRCYKADS ARGEEASCIS
CYMRDNPGST QEDALNLING MIEDMIKKLN WEFLRPDNNA PISSKKHAFN ISRGLHHFYN
YRDGYSVASK ETKDLVIKTV LEPVLM
