ID   TSGD1_ZINOF             Reviewed;         550 AA.
AC   Q0VHD6;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=(+)-germacrene D synthase;
DE            EC=4.2.3.77;
OS   Zingiber officinale (Ginger) (Amomum zingiber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=94328;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Rhizome;
RX   PubMed=16839518; DOI=10.1016/j.abb.2006.06.007;
RA   Picaud S., Olsson M.E., Brodelius M., Brodelius P.E.;
RT   "Cloning, expression, purification and characterization of recombinant (+)-
RT   germacrene D synthase from Zingiber officinale.";
RL   Arch. Biochem. Biophys. 452:17-28(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of germacrene D. Can use
CC       farnesyl diphosphate as substrate, but not geranyl diphosphate.
CC       Produces mainly (+)-germacrene D along with germacrene B and a number
CC       of minor by-products. {ECO:0000269|PubMed:16839518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate;
CC         Xref=Rhea:RHEA:30427, ChEBI:CHEBI:33019, ChEBI:CHEBI:49046,
CC         ChEBI:CHEBI:175763; EC=4.2.3.77;
CC         Evidence={ECO:0000269|PubMed:16839518};
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       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC       Note=Magnesium, manganese, cobalt or nickel, but not zinc or copper.
CC       Binds 3 magnesium ions per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.88 uM for (2E,6E)-farnesyl diphosphate (in presence of
CC         magnesium) {ECO:0000269|PubMed:16839518};
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:16839518};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY860846; AAX40665.1; -; mRNA.
DR   AlphaFoldDB; Q0VHD6; -.
DR   SMR; Q0VHD6; -.
DR   KEGG; ag:AAX40665; -.
DR   BioCyc; MetaCyc:MON-13556; -.
DR   BRENDA; 4.2.3.71; 6754.
DR   BRENDA; 4.2.3.77; 6754.
DR   UniPathway; UPA00213; -.
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..550
FT                   /note="(+)-germacrene D synthase"
FT                   /id="PRO_0000413960"
FT   MOTIF           304..308
FT                   /note="DDXXD motif"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         455
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  63755 MW;  6FFD9F668E648F7F CRC64;
     MENQSLTFVG DEEAKVRKST KFHPSIWGDY FIQNSSLSHA EESTQRMIKR VEELKVQVKS
     MFKDTSDILQ LMNLIDSIQM LGLDYHFENE IDKALRLINE VDDKSYGLYE TSLRFRLLRQ
     HGNHVSTDIF NKFKGDNGSF ISSLNGDAKG LLSLYNASYL GTHGETILDE AKSFAKPQLI
     SLLSELEQSL AAQVTLFLEL PLHKRVKILL VRKYILIYQE GAMRNNVLLE FAKLNFNLLQ
     SLYQEELKKI SIWWYDLALA KSLSFTRDRI VECYYWVLTL YFDPQYSHSR LIYSKVISLV
     SIMDDIYDNY GTLEECRQLT EAIKRWKPQA IDSLPEYLKY FYLKLLKTFE EIGEELEHNE
     KYRMLYLQDQ IKAIAVAYLE EAKWSIERHV PSLDEHLHYS LITSGCSLVP CASYVGMGEV
     ATKEVFDWHS SFPKAVEACC AIGRILNDIT SYEREQGRGD NASTVESYMK DHGTNEKDAC
     KKLQEIVEKA WKDLNQESLN QKNISRLIIE RLVNFSRSME EIYMSNDMYT NSGTKMKGNI
     TLVLVEAFPV