3CAR1_PICSI
ID 3CAR1_PICSI Reviewed; 627 AA.
AC F1CKI6; C0PSU3; F1CKI7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=(+)-3-carene synthase 1, chloroplastic {ECO:0000303|PubMed:21323772, ECO:0000303|PubMed:21385377};
DE EC=4.2.3.107 {ECO:0000269|PubMed:21323772};
DE AltName: Full=(+)-car-3-ene synthase 1 {ECO:0000303|PubMed:21323772};
DE AltName: Full=3-carene cyclase 1 {ECO:0000303|PubMed:21323772};
DE AltName: Full=Terpene synthase TPS-3car1 {ECO:0000303|PubMed:21323772, ECO:0000303|PubMed:21385377};
DE Short=PsTPS-3car1 {ECO:0000303|PubMed:21323772, ECO:0000303|PubMed:21385377};
DE Flags: Precursor;
GN Name=TPS-3car1 {ECO:0000303|PubMed:21323772, ECO:0000303|PubMed:21385377};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RC STRAIN=cv. FB3-425;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY
RP JASMONIC ACID, BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS VAL-190 AND GLU-473,
RP AND PATHWAY.
RC STRAIN=cv. H898, and cv. Q903;
RX PubMed=21323772; DOI=10.1111/j.1365-313x.2010.04478.x;
RA Hall D.E., Robert J.A., Keeling C.I., Domanski D., Quesada A.L.,
RA Jancsik S., Kuzyk M.A., Hamberger B., Borchers C.H., Bohlmann J.;
RT "An integrated genomic, proteomic and biochemical analysis of (+)-3-carene
RT biosynthesis in Sitka spruce (Picea sitchensis) genotypes that are
RT resistant or susceptible to white pine weevil.";
RL Plant J. 65:936-948(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. FB3-425; TISSUE=Bark;
RA Reid K.E., Liao N., Ralph S., Kolosova N., Oddy C., Moore R., Mayo M.,
RA Wagner S., King J., Yanchuk A., Holt R., Jones S., Marra M., Ritland C.E.,
RA Ritland K., Bohlmann J.;
RT "Full length sequence-verified cDNA sequences from Sitka spruce (Picea
RT sitchensis).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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 (e.g. insect attack by white
CC pine weevil P.strobi) and pathogens (PubMed:21385377, PubMed:21323772).
CC Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-car-
CC 3-ene (PubMed:21385377, PubMed:21323772). {ECO:0000269|PubMed:21323772,
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:21323772};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.88 uM for geranyl diphosphate {ECO:0000269|PubMed:21323772};
CC Vmax=32.1 pmol/sec/ug enzyme with geranyl diphosphate as substrate
CC {ECO:0000269|PubMed:21323772};
CC Note=kcat is 2.21 sec(-1) with geranyl diphosphate as substrate.
CC {ECO:0000269|PubMed:21323772};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21323772}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:21323772}.
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 -!- MISCELLANEOUS: Expressed in both resistant and susceptible trees.
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; HQ426167; ADZ45511.1; -; mRNA.
DR EMBL; HQ336798; ADU85924.1; -; mRNA.
DR EMBL; HQ336799; ADU85925.1; -; mRNA.
DR EMBL; BT071423; ACN40883.1; -; mRNA.
DR AlphaFoldDB; F1CKI6; -.
DR SMR; F1CKI6; -.
DR PRIDE; F1CKI6; -.
DR KEGG; ag:ADU85924; -.
DR BRENDA; 4.2.3.107; 8974.
DR BRENDA; 4.2.3.113; 8974.
DR SABIO-RK; F1CKI6; -.
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; 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:0043693; P:monoterpene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP: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; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..627
FT /note="(+)-3-carene synthase 1, chloroplastic"
FT /id="PRO_0000418967"
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"
FT VARIANT 190
FT /note="M -> V (in strain: cv. Q903; susceptibility to
FT pathogens)"
FT /evidence="ECO:0000269|PubMed:21323772"
FT VARIANT 473
FT /note="V -> E (in strain: cv. Q903; susceptibility to
FT pathogens)"
FT /evidence="ECO:0000269|PubMed:21323772"
FT CONFLICT 22
FT /note="S -> F (in Ref. 1; ADZ45511 and 3; ACN40883)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="P -> T (in Ref. 1; ADZ45511 and 3; ACN40883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 72037 MW; 62E3FF3D350981E5 CRC64;
MSVISIVPLA SKPCLYKSFI SSTHEPKALR RPISTVGLCR RAKSVTASMS MSSSTALSDD
GVQRRIGNHH SNLWDDNFIQ SLSSPYGASS YAERAERLIG EVKEIFNRIS MANGELVSHV
DDLLQHLSMV DNVERLGIDR HFQTEIKVSL DYVYSYWSEK GIGPGRDIVC ADLNTTALGF
RLLRLHGYTM FPDVFEQFKD QMGRIACSTN QTERQISSIL NLFRASLIAF PWEKVMEEAE
IFSTAYLKEA LQTIPVSSLS REIQYVLDYR WHSDLPRLET RTYIDILREN ATNETLDMKT
EKLLELAKVE FNIFNSLQQN ELKCVSRWWK ESGSPDLTFI RHRQVEFYTL VSGIDMEPKR
STFRINFVKI CHFVTILDDM YDTFGTIDEL RLFTAAVKRW DKSATECLPE YMKGVYIDLY
ETVNELAREA YKSQGRDTLN YARQALEDYL GSYLKEAEWI STGYIPTFEE YLVNGKVSSA
HRIATLQPIL MLDVPFPPHV LQEIDFPSKF NDLAGSILRL RGDTRCYQND RARGEEASCI
SCYMKDNPGS TEEDALNHIN GMIEKQIKEL NWELLKPDKN VPISSKKHAF NISRGLHHFY
KYRDGYTVAN SETRNLVIKT VLEPVPM
