CAMPS_PINCO
ID CAMPS_PINCO Reviewed; 619 AA.
AC R9QMY8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=(-)-camphene synthase, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.117 {ECO:0000269|PubMed:23679205};
DE AltName: Full=(+)-alpha-pinene synthase 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.121 {ECO:0000269|PubMed:23679205};
DE AltName: Full=(-)-alpha-pinene synthase 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.119 {ECO:0000269|PubMed:23679205};
DE AltName: Full=(-)-beta-pinene synthase (-)camp/(+)alphapin1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.120 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Myrcene synthase (-)camp/(+)alphapin1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.15 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Terpene synthase (-)camp/(+)alphapin1 {ECO:0000303|PubMed:23679205};
DE Short=PcTPS-(-)camp/(+)alphapin1 {ECO:0000303|PubMed:23679205};
DE AltName: Full=Tricyclene synthase (-)camp/(+)alphapin1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.105 {ECO:0000269|PubMed:23679205};
DE Flags: Precursor;
GN Name=TPS-(-)camp/(+)Apin1 {ECO:0000303|PubMed:23679205};
GN Synonyms=TPS-(-)camp {ECO:0000303|PubMed:23679205};
OS Pinus contorta (Shore pine) (Lodgepole pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3339;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23679205; DOI=10.1186/1471-2229-13-80;
RA Hall D.E., Yuen M.M.S., Jancsik S., Quesada A.L., Dullat H.K., Li M.,
RA Henderson H., Arango-Velez A., Liao N.Y., Docking R.T., Chan S.K.,
RA Cooke J.E.K., Breuil C., Jones S.J.M., Keeling C.I., Bohlmann J.;
RT "Transcriptome resources and functional characterization of monoterpene
RT synthases for two host species of the mountain pine beetle, lodgepole pine
RT (Pinus contorta) and jack pine (Pinus banksiana).";
RL BMC Plant Biol. 13:80-80(2013).
CC -!- FUNCTION: Monoterpene 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:23679205). Catalyzes the conversion of (2E)-geranyl diphosphate
CC (GPP) to (-)-camphene, (+)-alpha-pinene and (-)-alpha-pinene, and, to a
CC lower extent, to tricyclene, myrcene and (-)-beta-pinene
CC (PubMed:23679205). {ECO:0000269|PubMed:23679205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,4R)-camphene + diphosphate;
CC Xref=Rhea:RHEA:25484, ChEBI:CHEBI:89, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.117;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25485;
CC Evidence={ECO:0000269|PubMed:23679205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1R,5R)-alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:32575, ChEBI:CHEBI:28261, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.121;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32576;
CC Evidence={ECO:0000269|PubMed:23679205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + tricyclene;
CC Xref=Rhea:RHEA:32687, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64266; EC=4.2.3.105;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32688;
CC Evidence={ECO:0000269|PubMed:23679205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:23679205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate;
CC Xref=Rhea:RHEA:25496, ChEBI:CHEBI:28359, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.120;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25497;
CC Evidence={ECO:0000269|PubMed:23679205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.119;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25489;
CC Evidence={ECO:0000269|PubMed:23679205};
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:23679205}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:23679205}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; JQ240299; AFU73851.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102703; F:camphene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IDA:UniProtKB.
DR GO; GO:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0102701; F:tricyclene synthase activity; IDA:UniProtKB.
DR GO; GO:0018867; P:alpha-pinene metabolic process; 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:0016114; P:terpenoid 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..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..619
FT /note="(-)-camphene synthase, chloroplastic"
FT /id="PRO_0000455027"
FT MOTIF 370..374
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 522
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 619 AA; 71300 MW; 8B0538033D5E5C6E CRC64;
MALVSVAPLV SMRRSLFSSP YELKSIDKTI PNLVMCRKRM SGTPSIRVSS TTSASNDDGV
RRRVGDYRYN HWDDDLIDSL ATSYEAPSYL ERADTLVEAI KDRFNSMGVE DGERISPLTD
LYQRLWMVDS VERLGIDRHF QNEIKSALDY VFSYWKEKGI GRGRQSAVTD LNSTALGFRT
LRLHGYPVSS DVLENFKDHN GQFTCSGIQT EGEIRGVLNL FRASLIAFPG EKVMEEAEIF
STMYLKHALQ KIAVSSLSQE IEYLLDYGWH TNLPRLEARM YMDVFPQDTI YEQKLVELAK
VEFNIFHSLQ KRELQSLTRW WKHYGFPQLS FTRHIHVEYY TFASCVATDP KQSAFRLGFA
KMSHFVTVLD DIYDTYGTME ELELFTAAIK RWDPSLVDCL PEYMKGVYMA VYDTVNEMAK
EAEKVQGRDT LNYVRQAWEP YFDAYMIEAK WISSGYLPTF QEYLDNSKIS FGSRITILQP
ILTLGEPLPH EILQEIDFPS KFNDLISVLL RLKGDTRCYK ADRARGEEAS SVSCYMKDNA
GLTEEDAIHR INAMVHNLLK ELNWELLKPD CNVPISCKKA AFDICRIFHH GYKYRDGYGD
ATIETKNLVK RTVLEPVPL
