3CAR1_PICXS
ID 3CAR1_PICXS Reviewed; 627 AA.
AC F2XF94;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=(+)-3-carene synthase 1, chloroplastic {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.107 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Far/Oci {ECO:0000303|PubMed:21385377};
DE Short=PgxeTPS-Car1 {ECO:0000303|PubMed:21385377};
DE Flags: Precursor;
GN Name=TPS-3car1 {ECO:0000303|PubMed:21385377};
OS Picea engelmannii x Picea glauca (Hybrid white spruce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=373101;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. Fa1-1028;
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).
CC -!- FUNCTION: Terpene 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:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate
CC (GPP) to (+)-car-3-ene (PubMed:21385377).
CC {ECO:0000269|PubMed:21385377}.
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: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 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:21385377}.
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:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ426152; ADZ45510.1; -; mRNA.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid 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..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..627
FT /note="(+)-3-carene synthase 1, chloroplastic"
FT /id="PRO_0000454411"
FT MOTIF 378..382
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 627 AA; 72078 MW; 901E702DE50BC5C6 CRC64;
MSVISIVPLV SKPCLYKSFI SSTHEPKALR RPISTVGLCR RAKSVTASMS MSSSTALSDD
GVQRRIGNHH SNLWDDNFIQ SLSSPYGASS YAERAERLIG 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 YDTFGTMDEL RLFTAAVKRW DKSATECLPE YMKGVYIDLY
ETVNELAREA YKSQGRDTLN YARQALEDYL GSYLKEAEWI STGYIPTFEE YLENGKVSSA
HRIATLQPIL MLDVPFPPHV LQEIDFPSKF NDLAGSILRL RGDTRCYQND RARGEEASCI
SCYMKDNPGS TEKEALNHIN GMIEKRIKEL NWELLKPDKN VPISSKKHAF NISRGLHHFY
KYRDGYTVAN SETRNLVIKT VLEPVPM
