PINS_LAVST
ID PINS_LAVST Reviewed; 600 AA.
AC T1RRL8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Alpha pinene synthase, chloroplastic {ECO:0000303|PubMed:24943828};
DE Short=LsPINS {ECO:0000303|PubMed:24943828};
DE EC=4.2.3.- {ECO:0000250|UniProtKB:T1RRI8};
DE Flags: Precursor;
GN Name=PINS {ECO:0000303|PubMed:24943828};
OS Lavandula stoechas (Butterfly lavender).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Lavandulinae;
OC Lavandula.
OX NCBI_TaxID=39333;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=24943828; DOI=10.1111/ppl.12241;
RA Benabdelkader T., Guitton Y., Pasquier B., Magnard J.L., Jullien F.,
RA Kameli A., Legendre L.;
RT "Functional characterization of terpene synthases and chemotypic variation
RT in three lavender species of section Stoechas.";
RL Physiol. Plantarum 153:43-57(2015).
CC -!- FUNCTION: Monoterpene synthase involved in the biosynthesis of volatile
CC compounds widely used in aromatherapy and folk medicine, and present in
CC culinary herbs (PubMed:24943828). Mediates the conversion of (2E)-
CC geranyl diphosphate (GPP) into alpha-pinene and, as minor compounds,
CC into alpha-phellandrene, limonene and alpha-terpinolene (By
CC similarity). {ECO:0000250|UniProtKB:T1RRI8,
CC ECO:0000269|PubMed:24943828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000250|UniProtKB:T1RRI8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663;
CC Evidence={ECO:0000250|UniProtKB:T1RRI8};
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: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000250|UniProtKB:T1RRI8}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Barely detectable in leaves.
CC {ECO:0000269|PubMed:24943828}.
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:0000250|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; JX501515; AGN72802.1; -; mRNA.
DR SMR; T1RRL8; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
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:0046248; P:alpha-pinene biosynthetic 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:0016099; P:monoterpenoid 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 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..600
FT /note="Alpha pinene synthase, chloroplastic"
FT /id="PRO_0000454961"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 354..358
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 600 AA; 70225 MW; 1C722716C1A8A8E9 CRC64;
MSSISMHARP LNISAANNHH PSWDRRVSKP RRVAAKHLRL RLSCSLQLDG KPLDETRRSA
NYQPSAWDFN FIQSLHNQYK EDKYVTRHTE LTAQVKMLLE EETDAVQQLD LIEDLKNLGI
NYLFKDKIQQ ILNHIYNQHR CFQNNQVEGN DLYFTALGFR LLRQHGFEVS QEVFDRFTNE
EGTDFNPSLI DDTKGLLQLY EASFLLREGE DTLELARQFS TKLLQKKVDE DGDREVGDNL
LVWIRHSLEL PLHWRIHRIE ARWFLDAYAT RHDMNPIIFE LAKLDFNITQ ATQQEELRDL
SRWWNSAGLV EKLSFARDRV VESYFWAIGT LEPRQYGYQR KLVAKIIALI SVVDDVYDIY
GTLDELKLFT DVMRRWDAES FDQLPYYMKI CYLIINNFIF ELAYDILKDK GFNSLSYLQR
SWLDVVEGYF TEAKWYYSGY TPNLEEYLKN AKITVTCPMI LSQIYFTIAS SIEKPELESM
YKYHDILYLS GLLLRLPDDL GTALHELKRG DVPKAMQCYM KEKNVPEKEA REHVRFLIRE
ASKQMNTVSA ADCPFPDDFV AAAANLGRVA NFVYVDGDGF GDQHSKMLQQ IAALMFEPYD
