TPSD3_ABIGR
ID TPSD3_ABIGR Reviewed; 628 AA.
AC O24475; Q94FW0;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pinene synthase, chloroplastic;
DE EC=4.2.3.119;
DE EC=4.2.3.120;
DE AltName: Full=(-)-(1S,5S)-pinene synthase;
DE AltName: Full=Agg-pin1;
DE AltName: Full=Beta-geraniolene synthase;
DE Flags: Precursor;
GN Name=ag3; Synonyms=AG3.18;
OS Abies grandis (Grand fir) (Pinus grandis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX NCBI_TaxID=46611;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, CATALYTIC ACTIVITY, AND
RP CHARACTERIZATION.
RX PubMed=9268308; DOI=10.1074/jbc.272.35.21784;
RA Bohlmann J., Steele C.L., Croteau R.B.;
RT "Monoterpene synthases from grand fir (Abies grandis). cDNA isolation,
RT characterization, and functional expression of myrcene synthase, (-)-(4S)-
RT limonene synthase, and (-)-(1S,5S)-pinene synthase.";
RL J. Biol. Chem. 272:21784-21792(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-628, AND NOMENCLATURE.
RX PubMed=11404343; DOI=10.1093/genetics/158.2.811;
RA Trapp S.C., Croteau R.B.;
RT "Genomic organization of plant terpene synthases and molecular evolutionary
RT implications.";
RL Genetics 158:811-832(2001).
RN [3]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX PubMed=9539701; DOI=10.1073/pnas.95.8.4126;
RA Bohlmann J., Meyer-Gauen G., Croteau R.B.;
RT "Plant terpenoid synthases: molecular biology and phylogenetic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998).
CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC response to insect attack or other injury. Involved in monoterpene
CC (C10) olefins biosynthesis. A mixture of alpha- and beta-pinene is
CC produced by this enzyme. {ECO:0000269|PubMed:9539701}.
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:9268308};
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:9268308};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:9268308}.
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 -!- MISCELLANEOUS: The conserved 64-Arg-Arg-65 motif may play a role in the
CC isomerization step of the terpenoid cyclization reaction sequence.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; U87909; AAB71085.1; -; mRNA.
DR EMBL; AF326517; AAK83564.1; -; Genomic_DNA.
DR AlphaFoldDB; O24475; -.
DR SMR; O24475; -.
DR KEGG; ag:AAB71085; -.
DR BioCyc; MetaCyc:MON-12819; -.
DR BRENDA; 4.2.3.119; 2.
DR BRENDA; 4.2.3.120; 2.
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:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..628
FT /note="Pinene synthase, chloroplastic"
FT /id="PRO_0000033628"
FT MOTIF 379..383
FT /note="DDXXD motif"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 103
FT /note="K -> E (in Ref. 2; AAK83564)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="E -> G (in Ref. 2; AAK83564)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="V -> A (in Ref. 2; AAK83564)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="L -> F (in Ref. 2; AAK83564)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="Q -> H (in Ref. 2; AAK83564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 71506 MW; 23DBB788F3C8072C CRC64;
MALVSTAPLA SKSCLHKSLI SSTHELKALS RTIPALGMSR RGKSITPSIS MSSTTVVTDD
GVRRRMGDFH SNLWDDDVIQ SLPTAYEEKS YLERAEKLIG EVKNMFNSMS LEDGELMSPL
NDLIQRLWIV DSLERLGIHR HFKDEIKSAL DYVYSYWGEN GIGCGRESVV TDLNSTALGL
RTLRLHGYPV SSDVFKAFKG QNGQFSCSEN IQTDEEIRGV LNLFRASLIA FPGEKIMDEA
EIFSTKYLKE ALQKIPVSSL SREIGDVLEY GWHTYLPRLE ARNYIQVFGQ DTENTKSYVK
SKKLLELAKL EFNIFQSLQK RELESLVRWW KESGFPEMTF CRHRHVEYYT LASCIAFEPQ
HSGFRLGFAK TCHLITVLDD MYDTFGTVDE LELFTATMKR WDPSSIDCLP EYMKGVYIAV
YDTVNEMARE AEEAQGRDTL TYAREAWEAY IDSYMQEARW IATGYLPSFD EYYENGKVSC
GHRISALQPI LTMDIPFPDH ILKEVDFPSK LNDLACAILR LRGDTRCYKA DRARGEEASS
ISCYMKDNPG VSEEDALDHI NAMISDVIKG LNWELLKPDI NVPISAKKHA FDIARAFHYG
YKYRDGYSVA NVETKSLVTR TLLESVPL
