RAPN1_PINCO
ID RAPN1_PINCO Reviewed; 628 AA.
AC R9QMW2;
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=4.2.3.121 {ECO:0000269|PubMed:23679205};
DE AltName: Full=Terpene synthase (+)alphapin1 {ECO:0000303|PubMed:23679205};
DE Short=PcTPS-(+)alphapin1 {ECO:0000303|PubMed:23679205};
DE Flags: Precursor;
GN Name=TPS-(+)Apin1 {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 (+)-alpha-pinene (PubMed:23679205).
CC {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 -!- 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; JQ240295; AFU73847.1; -; mRNA.
DR BRENDA; 4.2.3.121; 4843.
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..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..628
FT /note="(+)-alpha pinene synthase 1, chloroplastic"
FT /id="PRO_0000455026"
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; 71551 MW; 2FCCA0FDE495A980 CRC64;
MALVSAVPLN SKLCLCRTLF GFSHELKAIH STVPNLGMCR GGKSIAPSMS MSSTTSVSNE
DGVPRRIAGH HSNLWDDDSI ASLSTSYEAP SYRERADRVI GEVKNIFDLM SVEDGVFTSP
LSDLHHRLWM VDSVERLGID RHFKHEINSA LDHVYSYWTE KGIGRGRESG VTDLNSTALG
LRTLRLHGYT VSSHVLDHFK NEKGQFTWSA IQTEGEIRDV LNLFRASLIA FPGEKIMEAA
EIFSTMYLKD ALQKIPPSGL SQEIEYLLEF GWHTNLPRME TRMYIDVFGE DTTFETPYLI
REKLLELAKL EFNIFHSLVK RELQSLTRWW KDYGFPEITF SRHRHVEYYT LAACIANDPK
HSAFRLGFGK ISHMITILDD IYDTFGTMEE LELLTAAFKR WDPSSIECLP DYMKGVYMAV
YDNINEMARE AQKIQGWDTV SYARKSWEAF IGAYIQEAKW ISSGYLPTFD EYLENGKVSF
GSRITTLEPM LTLGFPLPPR ILQEIDFPSK FNDLTCAILR LKGDTQCYKA DRARGEEASA
VSCYMKDHPG ITEEDAVNQV NAMVDNLTKE LNWELLRPDS GVPISYKKVA FDICRVFHYG
YKYRDGFSVA SVEIKNLVTR TVVETVPL
