TPSD4_ABIGR
ID TPSD4_ABIGR Reviewed; 581 AA.
AC O64404; Q94FW3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Delta-selinene synthase;
DE EC=4.2.3.71 {ECO:0000269|PubMed:9442047};
DE EC=4.2.3.76 {ECO:0000269|PubMed:9442047};
DE AltName: Full=Agfdsel1;
GN Name=ag4;
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, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9442047; DOI=10.1074/jbc.273.4.2078;
RA Steele C.L., Crock J., Bohlmann J., Croteau R.B.;
RT "Sesquiterpene synthases from grand fir (Abies grandis). Comparison of
RT constitutive and wound-induced activities, and cDNA isolation,
RT characterization, and bacterial expression of delta-selinene synthase and
RT gamma-humulene synthase.";
RL J. Biol. Chem. 273:2078-2089(1998).
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 34 sesquiterpene
CC (C15) olefins biosynthesis. {ECO:0000269|PubMed:9442047,
CC ECO:0000269|PubMed:9539701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1E,4E)-germacrene B +
CC diphosphate; Xref=Rhea:RHEA:25444, ChEBI:CHEBI:5337,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.71;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-delta-selinene +
CC diphosphate; Xref=Rhea:RHEA:30423, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49279, ChEBI:CHEBI:175763; EC=4.2.3.76;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-guaia-6,9-diene +
CC diphosphate; Xref=Rhea:RHEA:25448, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49204, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for farnesyl diphosphate {ECO:0000269|PubMed:9442047};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Constitutive expression.
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: In sesquiterpene synthases utilizing farnesyl
CC diphosphate as substrate, magnesium is more efficient as cofactor than
CC is manganese.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; U92266; AAC05727.1; -; mRNA.
DR EMBL; AF326513; AAK83561.1; -; Genomic_DNA.
DR AlphaFoldDB; O64404; -.
DR SMR; O64404; -.
DR KEGG; ag:AAC05727; -.
DR BioCyc; MetaCyc:AG4-MON; -.
DR BRENDA; 4.2.3.60; 2.
DR BRENDA; 4.2.3.71; 2.
DR BRENDA; 4.2.3.76; 2.
DR SABIO-RK; O64404; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0005737; C:cytoplasm; 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 Cytoplasm; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..581
FT /note="Delta-selinene synthase"
FT /id="PRO_0000186447"
FT MOTIF 331..335
FT /note="DDXXD motif"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 41
FT /note="L -> I (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 54..62
FT /note="LTEMEMDDG -> SIEMEDS (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> S (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..92
FT /note="QTA -> ETT (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="G -> D (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> S (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Q -> R (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="N -> T (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..203
FT /note="AGH -> TGR (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..211
FT /note="VDQ -> LDE (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="L -> I (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="H -> Q (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="Q -> D (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="K -> N (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 302..307
FT /note="SWVVMC -> FWAVIG (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 325..326
FT /note="IL -> TV (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="V -> I (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..343
FT /note="HEI -> DEL (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 358..359
FT /note="TD -> IH (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 375..377
FT /note="TVN -> IAD (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="V -> F (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="R -> Q (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="T -> A (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="T -> S (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="I -> M (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="M -> L (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="M -> L (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="L -> V (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="D -> G (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..467
FT /note="LDLL -> QELS (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="A -> T (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="I -> L (in Ref. 2; AAK83561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 67968 MW; 864622AE8BCC32C8 CRC64;
MAEISESSIP RRTGNHHGNV WDDDLIHSLN SPYGAPAYYE LLQKLIQEIK HLLLTEMEMD
DGDHDLIKRL QIVDTLECLG IDRHFEHEIQ TAALDYVYRW WNEKGIGEGS RDSFSKDLNA
TALGFRALRL HRYNVSSGVL KNFKDENGKF FCNFTGEEGR GDKQVRSMLS LLRASEISFP
GEKVMEEAKA FTREYLNQVL AGHGDVTDVD QSLLREVKYA LEFPWHCSVP RWEARSFLEI
YGHNHSWLKS NINQKMLKLA KLDFNILQCK HHKEIQFITR WWRDSGISQL NFYRKRHVEY
YSWVVMCIFE PEFSESRIAF AKTAILCTVL DDLYDTHATL HEIKIMTEGV RRWDLSLTDD
LPDYIKIAFQ FFFNTVNELI VEIVKRQGRD MTTIVKDCWK RYIESYLQEA EWIATGHIPT
FNEYIKNGMA SSGMCILNLN PLLLLDKLLP DNILEQIHSP SKILDLLELT GRIADDLKDF
EDEKERGEMA SSLQCYMKEN PESTVENALN HIKGILNRSL EEFNWEFMKQ DSVPMCCKKF
TFNIGRGLQF IYKYRDGLYI SDKEVKDQIF KILVHQVPME E
