3CAR1_PICAB
ID 3CAR1_PICAB Reviewed; 627 AA.
AC Q84SM8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Carene synthase, chloroplastic;
DE Short=PaJF67;
DE Short=PaTPS-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=JF67;
OS Picea abies (Norway spruce) (Picea excelsa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP JASMONIC ACID.
RX PubMed=12602896; DOI=10.1023/a:1020714403780;
RA Faeldt J., Martin D., Miller B., Rawat S., Bohlmann J.;
RT "Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-
RT induced terpene synthase gene expression, and cDNA cloning and functional
RT characterization of (+)-3-carene synthase.";
RL Plant Mol. Biol. 51:119-133(2003).
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:12602896}.
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:12602896};
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 -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:12602896}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; AF461460; AAO73863.1; -; mRNA.
DR AlphaFoldDB; Q84SM8; -.
DR SMR; Q84SM8; -.
DR KEGG; ag:AAO73863; -.
DR BioCyc; MetaCyc:MON-12775; -.
DR BRENDA; 4.2.3.107; 4815.
DR BRENDA; 4.2.3.113; 4815.
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:0071395; P:cellular response to jasmonic acid stimulus; IEP: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, chloroplastic"
FT /id="PRO_0000418971"
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; 71913 MW; B1B11AD15FC50F47 CRC64;
MSVISILPLA SKSCLYKSLM SSTHELKALC RPIATLGMCR RGKSVMASKS TSLTTAVSDD
GVQRRIGDHH SNLWDDNFIQ SLSSPYGASS YGERAERLIG EVKEIFNSLS RTDGELVSHV
DDLLQHLSMV DNVERLGIDR HFQTEIKVSL DYVYSYWSEK GIGSGRDIVC TDLNTTALGF
RILRLHGYTV FPDVFEHFKD QMGRIACSDN HTERQISSIL NLFRASLIAF PGEKVMEEAE
IFSATYLKEA LQTIPVSSLS QEIQYVLQYR WHSNLPRLEA RTYIDILQEN TKNQMLDVNT
KKVLELAKLE FNIFHSLQQN ELKSVSRWWK ESGFPDLNFI RHRHVEFYTL VSGIDMEPKH
CTFRLSFVKM CHLITVLDDM YDTFGTIDEL RLFTAAVKRW DPSTTECLPE YMKGVYTVLY
ETVNEMAQEA QKSQGRDTLS YVRQALEAYI GAYHKEAEWI SSGYLPTFDE YFENGKVSSG
HRIATLQPTF MLDIPFPHHV LQEIDFPSKF NDFACSILRL RGDTRCYQAD RARGEEASCI
SCYMKDNPGS TQEDALNHIN NMIEETIKKL NWELLKPDNN VPISSKKHAF DINRGLHHFY
NYRDGYTVAS NETKNLVIKT VLEPVPM
