SPIN1_PINBN
ID SPIN1_PINBN Reviewed; 623 AA.
AC R9QMW1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=(-)-alpha-pinene synthase 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.119 {ECO:0000269|PubMed:23679205};
DE AltName: Full=(-)-beta-phellandrene synthase (-)alpha/betapin1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.52 {ECO:0000269|PubMed:23679205};
DE AltName: Full=(-)-beta-pinene synthase 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.120 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Terpene synthase (-)alpha/betapin1 {ECO:0000303|PubMed:23679205};
DE Short=PbTPS-(-)alpha/betapin1 {ECO:0000303|PubMed:23679205};
DE Flags: Precursor;
GN Name=TPS-(-)A/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 (-)-alpha-pinene and (-)-beta-pinene, and, to a lower extent,
CC to (-)-beta-phellandrene (PubMed:23679205).
CC {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 -!- 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 = (-)-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; JQ240290; AFU73842.1; -; 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: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..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..623
FT /note="(-)-alpha-pinene synthase 1, chloroplastic"
FT /id="PRO_0000455022"
FT MOTIF 374..378
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
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 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 623 AA; 71422 MW; F21350B8259D1005 CRC64;
MDLISVLPSA SKSCVCLHKP LSSSTHKLKP FCKTIRILGM PRRWKFAGPS MSLSTVASDD
DIQRRTGGYH SNLWNDDVIQ FLSTPYGELA YRERAERLID EVRDIFSSMS LEDGEFSDLI
QRLWMVDNVE RLGIDRHFKN EIKSALDYVY SYWSEKGIGC GTKSIITNLN STALGFRTLR
LHGYPVSADV LKHFRNQIGQ FVSCPSETEE DIRSMVNLYR ASLIAFPGEE VMEEAERFSE
KYLKETLQKI PDCSLSREIG DVLEHGWHTN LPRLEARNYI DVFGQDTKNM ESNRKTEKLL
ELAKLEFNIF QSIQETELES LLRWWNDSGS PQITFTRHRH VEYYTLASCI AFEPQHSGFR
LGFAKACHII TVLDDMYDLF GTVDELKLFT AAIKRWDPSA TDCLPQYMKG IYMMVYNTVN
EMSAEAQKAQ GRDTLNYARQ AWEDCLDSYM QEAKWIATGF LPTFEEYLEN GKVSSAHRVS
ALQPMLTMDI PFPPHILKEV DFPSNLNDLA CAMLRLRGDT RCYQADRARG EETSCISCYM
KDNPGATEED ALNRLNVMIS GVIKELNWEL LKPDSGVPIS SKKINFDITR AFHYGYKYRD
GYSVSSVETK SFVMRTLLEP VPL
