SAPN1_PINBN
ID SAPN1_PINBN Reviewed; 629 AA.
AC R9QMY9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
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 pinene synthase 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE EC=4.2.3.120 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Terpene synthase (-)alphapin1 {ECO:0000303|PubMed:23679205};
DE Short=PbTPS-(-)alphapin1 {ECO:0000303|PubMed:23679205};
DE Flags: Precursor;
GN Name=TPS-(-)Apin1 {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, to a lower extent, to (-)-beta-pinene
CC (PubMed:23679205). {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 -!- 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; JQ240304; AFU73856.1; -; mRNA.
DR SMR; R9QMY9; -.
DR BRENDA; 4.2.3.119; 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..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..629
FT /note="(-)-alpha pinene synthase 1, chloroplastic"
FT /id="PRO_0000455023"
FT MOTIF 380..384
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 384
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 384
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 629 AA; 71713 MW; 0B0B80ED624DD8F5 CRC64;
MSPVSVISLP SDLCLPTSFI DRSGRELIPL HITIPNVAMR RQGKLMTRAS MSMNLRTAVS
DDAVIRRRGD FHSNLWDDDF IQSLSAPYGE PSYRERAERL IGEVKNSFNS MSNEDSESIT
PLDDLIQRLW MVDSVERLGI DRHFKKEIKS ALDHVYSYWS EKGIGCGRES VVTDLNSTAL
GLRTLRLHGY DVSAEVLNHF KNQSGQFACT LKQTEDQIRT VLNLYRASLI AFPGEKVMDE
AETFSAKYLK DALQKVPVSS LSREIGDVLE YGWHTYLPRL EARNYIDVFG QDTGNSQSYM
KTEKLLELAK LEFNIFHALQ KRELEYLVRW WKGSGSPQMT FCRHRHVEYY TLASCIAFEP
QHSGFRLGFA KACHIITVLD DMYDTFGTLD ELELFTSAIK RWDPSATECL PEYMKGVYMI
VYNTVNEMSQ EADKAQGRDT LNYCRQAWEE YIDAYMQEAK WIASGEVPTF EEYYENGKVS
SGHRVSALQP ILTTDIPFPE HVLKEVDIPS KLNDLASAIL RLRGDTRCYQ ADRARGEEAS
CISCYMKDNP GTTEEDALNH INAMISDVIK GLNWELLKPN SSVPISAKKH AFDISRAFHY
GYKYRDGYSV ASIETKSLVK RTVIDPVTL
