TPSD9_ABIGR
ID TPSD9_ABIGR Reviewed; 630 AA.
AC Q9M7D0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Terpinolene synthase, chloroplastic;
DE EC=4.2.3.113;
DE AltName: Full=Aggteo;
DE Flags: Precursor;
GN Name=ag9; Synonyms=agc9;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Stem;
RX PubMed=10441373; DOI=10.1006/abbi.1999.1332;
RA Bohlmann J., Phillips M., Ramachandiran V., Katoh S., Croteau R.B.;
RT "cDNA cloning, characterization, and functional expression of four new
RT monoterpene synthase members of the Tpsd gene family from grand fir (Abies
RT grandis).";
RL Arch. Biochem. Biophys. 368:232-243(1999).
RN [2]
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).
RN [3]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
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).
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:10441373,
CC ECO:0000269|PubMed:11404343, ECO:0000269|PubMed:9539701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
CC Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.113;
CC Evidence={ECO:0000269|PubMed:10441373};
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; Evidence={ECO:0000250};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
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 65-Arg-Arg-66 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; AF139206; AAF61454.1; -; mRNA.
DR AlphaFoldDB; Q9M7D0; -.
DR SMR; Q9M7D0; -.
DR KEGG; ag:AAF61454; -.
DR BioCyc; MetaCyc:AG9-MON; -.
DR BRENDA; 4.2.3.113; 2.
DR BRENDA; 4.2.3.119; 2.
DR BRENDA; 4.2.3.120; 2.
DR BRENDA; 4.2.3.16; 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..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..630
FT /note="Terpinolene synthase, chloroplastic"
FT /id="PRO_0000033631"
FT MOTIF 381..385
FT /note="DDXXD motif"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 630 AA; 72508 MW; 452437B87F203D8A CRC64;
MALVSILPLS SKSVLHKSWI VSTYEHKAIS RTIPNLGLRG RGKSVTHSLR MSLSTAVSDD
HGVQRRIVEF HSNLWDDDFI QSLSTPYGAP SYRERADRLI VEVKGIFTSI SAEDGELITP
LNDLIQRLLM VDNVERLGID RHFKNEIKAA LDYVYSYWNE KGIGSGSDSG VADLNSTALG
FRILRLHGYS VSSDVLEHFK EEKEKGQFVC SAIQTEEEIK SVLNLFRASL IAFPGEKVME
EAEIFSKIYL KEALQNIAVS SLSREIEYVL EDGWQTNMPR LETRNYIDVL GENDRDETLY
MNMEKLLEIA KLEFNIFHSL QQRELKDLSR WWKDSGFSHL TFSRHRHVEF YALASCIETD
RKHSGFRLGF AKMCHLITVL DDIYDTFGTM EELELFTAAF KRWDPSATDL LPEYMKGLYM
VVYETVNEIA READKSQGRE TLNDARRAWE AYLDSYMKEA EWISSGYLPT FEEYMETSKV
SFGYRIFALQ PILTMDVPLT HHILQEIDFP LRFNDLICSI LRLKNDTRCY KADRARGEEA
SCISCYMKEN PGSTEEDAIN HINAMVNNLI KEVNWELLRQ DGTAHIACKK HAFDILKGSL
HGYKYRDGFS VANKETKNWV RRTVLESVPL
