TPSDA_ABIGR
ID TPSDA_ABIGR Reviewed; 637 AA.
AC O22340; Q94FV9;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Limonene synthase, chloroplastic;
DE EC=4.2.3.16;
DE AltName: Full=(-)-(4S)-limonene synthase;
DE AltName: Full=Agg-lim1;
DE Flags: Precursor;
GN Name=ag10;
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, AND 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], 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. {ECO:0000269|PubMed:9539701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate;
CC Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.16;
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 70-Arg-Arg-71 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; AF006193; AAB70907.1; -; mRNA.
DR EMBL; AF326518; AAK83565.1; -; Genomic_DNA.
DR AlphaFoldDB; O22340; -.
DR SMR; O22340; -.
DR KEGG; ag:AAB70907; -.
DR BioCyc; MetaCyc:MON-12820; -.
DR BRENDA; 4.2.3.16; 2.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; 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..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..637
FT /note="Limonene synthase, chloroplastic"
FT /id="PRO_0000033632"
FT MOTIF 388..392
FT /note="DDXXD motif"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="L -> Q (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="G -> D (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="V -> L (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> Q (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> E (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="L -> E (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="E -> Q (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="A -> G (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="M -> I (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="I -> T (in Ref. 2; AAK83565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 73478 MW; 8E80CD9DDE886898 CRC64;
MALLSIVSLQ VPKSCGLKSL ISSSNVQKAL CISTAVPTLR MRRRQKALVI NMKLTTVSHR
DDNGGGVLQR RIADHHPNLW EDDFIQSLSS PYGGSSYSER AETVVEEVKE MFNSIPNNRE
LFGSQNDLLT RLWMVDSIER LGIDRHFQNE IRVALDYVYS YWKEKEGIGC GRDSTFPDLN
STALALRTLR LHGYNVSSDV LEYFKDEKGH FACPAILTEG QITRSVLNLY RASLVAFPGE
KVMEEAEIFS ASYLKKVLQK IPVSNLSGEI EYVLEYGWHT NLPRLEARNY IEVYEQSGYE
SLNEMPYMNM KKLLQLAKLE FNIFHSLQLR ELQSISRWWK ESGSSQLTFT RHRHVEYYTM
ASCISMLPKH SAFRMEFVKV CHLVTVLDDI YDTFGTMNEL QLFTDAIKRW DLSTTRWLPE
YMKGVYMDLY QCINEMVEEA EKTQGRDMLN YIQNAWEALF DTFMQEAKWI SSSYLPTFEE
YLKNAKVSSG SRIATLQPIL TLDVPLPDYI LQEIDYPSRF NELASSILRL RGDTRCYKAD
RARGEEASAI SCYMKDHPGS IEEDALNHIN AMISDAIREL NWELLRPDSK SPISSKKHAF
DITRAFHHVY KYRDGYTVSN NETKNLVMKT VLEPLAL
