BPHL1_PINCO
ID BPHL1_PINCO Reviewed; 621 AA.
AC R9QMR4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=(-)-beta-phellandrene synthase 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.52 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Terpene synthase (-)betaphell1 {ECO:0000303|PubMed:23679205};
DE Short=PcTPS-(-)betaphell1 {ECO:0000303|PubMed:23679205};
DE Flags: Precursor;
GN Name=TPS-(-)Bphell1 {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 (-)-beta-phellandrene and, to a lower extent, to (-)-alpha-
CC phellandrene (PubMed:23679205). {ECO:0000269|PubMed:23679205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (-)-beta-phellandrene +
CC diphosphate; Xref=Rhea:RHEA:25492, ChEBI:CHEBI:129,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.52;
CC Evidence={ECO:0000269|PubMed:23679205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25493;
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; JQ240301; AFU73853.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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: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..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..621
FT /note="(-)-beta-phellandrene synthase 1, chloroplastic"
FT /id="PRO_0000455015"
FT MOTIF 372..376
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 372
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 372
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 621 AA; 71452 MW; 2461B38A51B71A03 CRC64;
MALALVSVAP LVSMRRSLFS SPYELKSIDK TIPNLVMCRK RMSGTPSIRV SSTTSASNDD
GVRRRVGDYR YNHWDDDLID SLATSYEAPS YLERADTLVE AIKDRFNSMG VDDGERMSPL
TDLYQRLWMV DSVERLGIDR HFQNEIKSAL DYVFSYWKEK GIGRGRQSAV TDLNSTALGL
RTLRLHGYPV SSDVLENFKD HNGQFTCSGI QTEGEIRGVL NLFRASLIAF PGEKVMEEAE
IFSTMYLKHA LQKIAVSSLS QEIEYLLEYG WHTNPPRLEA RMYMEVFPQD TIYEQKLVEL
AKVEFNIFHS LQKRELQSLT RWWKHYGFPQ LSFTRHIHVE YYTFGSCIAT DPKQSAFRLC
FAKMSYFVTV LDDIYDTYGT MEELELFTAA IKRWDPSVVD CLPEYMKGVY MAVYDTVNEM
AKEAEKVQGR DTLNYVRQAW ELYIDAYMPE AKWISSGYLP TFQEYLDNSK ISFGTRITIL
QPILTLGEPL PHEILQEIDF PAKFNDLISV ILRLKGDTRC YKADRARGEE ASSVSCYMKD
NAGITEEDAV HCINDMVNNL LKELNWELLK PDSNVPISCR KAAFDICRIF HHGYKYRDGY
GDATIEVKNL VKRTVLEPVP L
