3CAR2_PICSI
ID 3CAR2_PICSI Reviewed; 627 AA.
AC F1CKI8; F1DI19;
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=Carene synthase 2, chloroplastic;
DE Short=PsTPS-3car2;
DE EC=4.2.3.107;
DE AltName: Full=(+)-car-3-ene synthase 2;
DE AltName: Full=3-carene cyclase 2;
DE Flags: Precursor;
GN Name=TPS-3car2;
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;
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 (e.g. white pine
CC weevil P.strobi) or other injury. {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 KM=1.47 uM for geranyl diphosphate {ECO:0000269|PubMed:21323772};
CC Vmax=0.91 pmol/sec/ug enzyme with geranyl diphosphate as substrate
CC {ECO:0000269|PubMed:21323772};
CC Note=kcat is 0.06 sec(-1) with geranyl diphosphate as substrate.
CC {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 resistant trees, not detected in
CC genomic DNA of susceptible trees.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ336800; ADU85926.1; -; mRNA.
DR EMBL; HQ850276; ADY38568.1; -; Genomic_DNA.
DR AlphaFoldDB; F1CKI8; -.
DR SMR; F1CKI8; -.
DR KEGG; ag:ADU85926; -.
DR BRENDA; 4.2.3.107; 8974.
DR BRENDA; 4.2.3.113; 8974.
DR SABIO-RK; F1CKI8; -.
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 2, chloroplastic"
FT /id="PRO_0000418968"
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; 71645 MW; E7F29AF18ED46620 CRC64;
MSVISIVPLA SKSCLYKSLM SSTHELKALC RPIVTLGMCR RGKSVMASMS TGLTTAVSDD
GVQRRIGDHH SNLWDDNFIQ SLSSPYRASS YGETTNKLIG EVKEIFNSLS MADGGLMSPV
DDLLQHLSMV DNVERLGIDR HFQTEIKVSL DYVYSYWSEK GIGSGRDIVC TDLNTTALGF
RILRLHGYTV FPDVFEHLKD QMGRIACSAN HTERQISSIL NLFRASLIAF PGEKVMEEAE
IFSATYLKEA LQTIPVSSLS QEIQYVLQYR WHSNLPRLEA RTYIDILQEN TKNQMLDVNT
EKVLELAKLE FNIFHSLQQN ELKSVSRWWK DSGFPDLNFI RHRHVEFYTL VSGIDMEPKH
STFRLSFVKM CHLITVLDDM YDTFGTIDEL RLFTAAVKRW DPSTTQCLPE YMKGVYIVLY
ETVNEMAKEA QKSQGRDTLN YVRQALEAYI GAYHKEAEWI STGYLPTFDE YFENGKASSG
HRIATLQPTF MLDIPFPHHI LQEIDFPSKF NDFACSILRL RGDTRCYQAD MARGEEASCI
SCYMKDNPGS TQEDALNHIN NMIEETIKKL NRELLKPDNN VPISSKKHAF DISRGLHHFY
NYRDGYTVAS NETKNLVIKT VLEPVPM
