3CAR3_PICSI
ID 3CAR3_PICSI Reviewed; 627 AA.
AC F1CKI9; F1CKJ0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Carene synthase 3, chloroplastic;
DE Short=PsTPS-3car3;
DE EC=4.2.3.107;
DE AltName: Full=(+)-car-3-ene synthase 3;
DE AltName: Full=3-carene cyclase 3;
DE Flags: Precursor;
GN Name=TPS-3car3;
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP INDUCTION BY JASMONIC ACID, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
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:21323772}.
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; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is less than 0.00001 sec(-1) with geranyl diphosphate as
CC substrate. {ECO:0000269|PubMed:21323772};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:21323772}.
CC -!- MISCELLANEOUS: Expressed only in susceptible trees.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ336801; ADU85927.1; -; Genomic_DNA.
DR EMBL; HQ336802; ADU85928.1; -; mRNA.
DR EMBL; HQ850277; ADY38569.1; -; Genomic_DNA.
DR AlphaFoldDB; F1CKI9; -.
DR SMR; F1CKI9; -.
DR PRIDE; F1CKI9; -.
DR KEGG; ag:ADU85927; -.
DR BRENDA; 4.2.3.107; 8974.
DR BRENDA; 4.2.3.113; 8974.
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:0043693; P:monoterpene 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; 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 3, chloroplastic"
FT /id="PRO_0000418969"
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"
FT VARIANT 285
FT /note="D -> H (in strain: cv. Q903; susceptibility to
FT pathogens)"
SQ SEQUENCE 627 AA; 71661 MW; ECEDE888EA373563 CRC64;
MSVISIVPLA SKSCLYKSLM SSTHELKALC RPIATLGMCR RGKSVMASMS TSLTTAVSDD
GVQRRIGHHH SNLWDDNFIQ SLSSPYGASS YAESAKKLIG EVKEIFNSLS MAAGGLMSPV
DDLLQHLSMV DNVERLGIDR HFQTEIKVSL DYVYSYWSEK GIGSGRDIVC TDLNTTALGF
RILRLHGYTV FPDVFEHFKD QMGRIACSAN HTERQISSIL NLFRASLIAF PGEKVMEEAE
IFSATYLKEA LQTIPVSSLS QEIQYVLQYR WHSNLPRLEA RTYIDILQEN TKNQMLDVNT
KKVLELAKLE FNIFHSLQQN ELKSVSRWWK ESGFPDLNFI RHRHVEFYTL VSGIDMEPKH
STFRLSFVKM CHLITVLDDM YDTFGTIDEL RLFTAAVKRW DPSTTQCLPE YMKGVYTVLY
ETVNEMAQEA QKSQGRDTLN YVRQALEAYI GAYHKEAEWI SSGYLPTFDE YFENGKVSSG
HRIATLQPIF MLDIPFPHHV LQEIDFPSNF NDFACSILRL RCDTRCYQAD RARGEEASCI
SCYMKDHPGS TQEDALNHIN NMIEETIKKL NWELMKPDNN VPISSKKPAF DISRGLHHFY
NYRDGYTVSS NETKNLVIKT VLEPVPM
