SBPN1_PINBN
ID SBPN1_PINBN Reviewed; 628 AA.
AC R9QMR0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=(-)-beta-pinene synthase 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.120 {ECO:0000269|PubMed:23679205};
DE AltName: Full=(-)-alpha-pinene synthase (-)betapin1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.119 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Terpene synthase (-)betapin1 {ECO:0000303|PubMed:23679205};
DE Short=PbTPS-(-)betapin1 {ECO:0000303|PubMed:23679205};
DE Flags: Precursor;
GN Name=TPS-(-)Bpin1 {ECO:0000303|PubMed:23679205};
OS Pinus banksiana (Jack pine) (Pinus divaricata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3353;
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-pinene and, to a lower extent, to (-)-alpha-pinene
CC (PubMed:23679205). {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; JQ240291; AFU73843.1; -; mRNA.
DR BRENDA; 4.2.3.120; 4842.
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:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene 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..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..628
FT /note="(-)-beta-pinene synthase 1, chloroplastic"
FT /id="PRO_0000455019"
FT MOTIF 379..383
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 628 AA; 71951 MW; E70AD2059356C152 CRC64;
MDLISVLPSA SKSCVCLHKP LSSSTHKLKP FCRTIRILGM PRPRKSVLMV SSMSISVNTL
VSDDAVQRRT GGYHSNLWND DVIQFLSTPY GELAYRERAE RLIDEVRNIF NSMSLEDGEF
SDLIIQRLWM VDNVERLGID RHFKNEIKSA LDYVYSYWSQ KGIGCGTKSI ITDLNSTALG
FRTLRLHGYP VSADVLKHFR NQIGQFVSCP SETEEDIRSM VNLYRASLIA FPGEEVMEEA
ESFSEKYLKE TLQKIPDCSL SREIGDVLEH GWHTNLPRFE ARNYIDVFGQ DTKNMESNRK
TEKLLELAKL EFNIFQSIQK TELESLLRWW NDSGSPQITF TRHRHVEYYT LASCIAFEPQ
HSGFRLGFAK ACHIITVLDD MYDLFGTVEE LKLFTAAIKR WDPSATDCLP QYMKGIYMMV
YNTVNEMSAE AQKAQGRDTL NYARQAWEVY LDSYVQEAKW IATGYLPTFE EYLENGKVSS
GHRVSALQPM LTMDIPFPPH ILKEVDFPSN LNDLACAILR LRGDTRCYQE DRARGEETSC
ISCYMKDNPG ATEEDALNHL NVMISGVIKE LNWELLKPDS SVPISSKKIN FDITRAFHYG
YKYRDGYSVS SVETKSLVMR TLLEPVPL
