ID   3CAR1_PICGL             Reviewed;         627 AA.
AC   C7ASI9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Carene synthase, chloroplastic;
DE            Short=PgTPS-3car;
DE            EC=4.2.3.107;
DE   AltName: Full=(+)-car-3-ene synthase;
DE   AltName: Full=3-carene cyclase;
DE   Flags: Precursor;
GN   Name=3CAR; ORFNames=PGB02;
OS   Picea glauca (White spruce) (Pinus glauca).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3330;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=cv. PG29;
RX   PubMed=19656416; DOI=10.1186/1471-2229-9-106;
RA   Hamberger B., Hall D., Yuen M., Oddy C., Hamberger B., Keeling C.I.,
RA   Ritland C., Ritland K., Bohlmann J.;
RT   "Targeted isolation, sequence assembly and characterization of two white
RT   spruce (Picea glauca) BAC clones for terpenoid synthase and cytochrome P450
RT   genes involved in conifer defence reveal insights into a conifer genome.";
RL   BMC Plant Biol. 9:106-106(2009).
CC   -!- FUNCTION: Terpene synthase (TPS) involved in defensive oleoresin
CC       formation in conifers in response to insect attack or other injury.
CC       {ECO:0000269|PubMed:19656416}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FJ609174; ACM04452.2; -; Genomic_DNA.
DR   AlphaFoldDB; C7ASI9; -.
DR   SMR; C7ASI9; -.
DR   KEGG; ag:ACM04452; -.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; ISS:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0043693; P:monoterpene biosynthetic process; ISS: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   3: Inferred from homology;
KW   Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..627
FT                   /note="Carene synthase, chloroplastic"
FT                   /id="PRO_0000418970"
FT   MOTIF           378..382
FT                   /note="DDXXD motif"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         530
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   627 AA;  71920 MW;  905D89F0A8C3E2AB CRC64;
     MSVISIMPLA SKPCLNKSFI SSTHEPKALR RPISTVGLCR RAKSVTASMS MSSSTAVSDD
     GVQRRIGNHH SNLWDDNFIQ SLSSPYGPSS YGERAERLIG EVKEIFNRIS MANGELVSHV
     DDLLQHLSMV DNVERLGIDR HFQTEIKVSL DYVYSYWSEK GIGPGRDIVC ADLNTTALGF
     RVLRLHGYTV FPDVFEQFKD QMGRIACSAN QTERQISSIL NLFRASLIAF PWEKVMEEAE
     IFSTAYLKEA LQTIPVSSLS REIQYVLDYR WHSDLPRLET RTYIDILREN ATNETLDMKT
     EKLLELAKVE FNIFNSLQQN ELKCVSRWWK ESGSPDLTFI RHRQVEFYTL VSGIDMEPKR
     STFRINFVKI CHFVTILDDM YDTFGTIDEL RLFTAAVTRW DKSATECLPE YMKGVYIDLY
     ETVNELAREA HKSQGRDTLN YAREALEDYL GSYLKEAEWI STGYIPTFEE YLENGKVSSA
     HRIATLQPIL MLDVPFPPHV LQEIDFPSKF NDLAGSILRL RGDTRCYQND RARGEEASCI
     SCYMKDNPGS TEEDALNHIN GMIEKQIKEL NWELLKPDKN VPISSKKHAF NISRGLHHFY
     KYRDGYTVAN SETRNLVIKT VLEPVPM