ID   GDS_OCIBA               Reviewed;         546 AA.
AC   Q5SBP6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Germacrene-D synthase;
DE            EC=4.2.3.75;
DE   AltName: Full=(-)-germacrene D synthase;
GN   Name=GDS;
OS   Ocimum basilicum (Sweet basil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC   Ocimum.
OX   NCBI_TaxID=39350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15516500; DOI=10.1104/pp.104.051318;
RA   Iijima Y., Davidovich-Rikanati R., Fridman E., Gang D.R., Bar E.,
RA   Lewinsohn E., Pichersky E.;
RT   "The biochemical and molecular basis for the divergent patterns in the
RT   biosynthesis of terpenes and phenylpropenes in the peltate glands of three
RT   cultivars of basil.";
RL   Plant Physiol. 136:3724-3736(2004).
CC   -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC       germacrene D from trans,trans-farnesyl diphosphate (FPP).
CC       {ECO:0000269|PubMed:15516500}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate;
CC         Xref=Rhea:RHEA:12016, ChEBI:CHEBI:33019, ChEBI:CHEBI:49044,
CC         ChEBI:CHEBI:175763; EC=4.2.3.75;
CC         Evidence={ECO:0000269|PubMed:15516500};
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   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY693644; AAV63786.1; -; mRNA.
DR   AlphaFoldDB; Q5SBP6; -.
DR   SMR; Q5SBP6; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0052577; F:germacrene-D synthase activity; IEA:RHEA.
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   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..546
FT                   /note="Germacrene-D synthase"
FT                   /id="PRO_0000399253"
FT   MOTIF           303..307
FT                   /note="DDXXD motif"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         448
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  63395 MW;  68B065512826AB6E CRC64;
     MTNMFASAAP ISTNNTTVED MRRSVTYHPS VWKDHFLDYA SGITEVEMEQ LQKQKERIKT
     LLAQTLDDFV LKIELIDAIQ RLGVGYHFEK EINHSLRQIY DTFQISSKDN DIRVVALRFR
     LLRQHGYPVP SDVFKKFIDN QGRLDESVMN NVEGMLSLYE ASNYGMEGED ILDKALEIST
     SHLEPLASRS RRINEALEMP ISKTLVRLGA RKFISIYEED ESRDEDLLKF AKLDFNILQK
     IHQEELTHIA RWWKELDLGN KLPFARDRVV ECYFWILGVY FEPQYNIARR FMTKVIAMTS
     IIDDIYDVHG TLEELQRFTD AIRSWDIRAI DELPPYMRLC YEALLGMYAE MENEMVKQNQ
     SYRIEYARQE MIKLVTTYME EAKWCYSKYI PNMDEYMKLA LVSGAYMMLA TTSLVGILGD
     PITKQDFDWI TNEPPILRAA SVICRLMDDV VGHGIEQKIS SVDCYMKENG CSKMEAVGEF
     SKRVKKAWKN LNEEWVEPRA ASMVILVRVV NLARVINLLY VGEDSYGNSS VKTKELIKGV
     LVHPIK