ID   TPS1_VALOF              Reviewed;         563 AA.
AC   J9RLZ7;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Germacrene C/D synthase;
DE            EC=4.2.3.60;
DE            EC=4.2.3.75;
DE   AltName: Full=Terpene synthase 1;
DE            Short=VoTPS1;
GN   Name=TPS1;
OS   Valeriana officinalis (Valerian) (Garden heliotrope).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Dipsacales; Caprifoliaceae; Valeriana.
OX   NCBI_TaxID=19953;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=22776156; DOI=10.1111/j.1742-4658.2012.08692.x;
RA   Pyle B.W., Tran H.T., Pickel B., Haslam T.M., Gao Z., MacNevin G.,
RA   Vederas J.C., Kim S.U., Ro D.K.;
RT   "Enzymatic synthesis of valerena-4,7(11)-diene by a unique sesquiterpene
RT   synthase from the valerian plant (Valeriana officinalis).";
RL   FEBS J. 279:3136-3146(2012).
CC   -!- FUNCTION: Mediates formation of germacrene C and germacrene D using
CC       farnesyl diphosphate as substrate. Can also catalyze formation of trace
CC       of germacrene B. {ECO:0000269|PubMed:22776156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene C;
CC         Xref=Rhea:RHEA:28302, ChEBI:CHEBI:33019, ChEBI:CHEBI:61478,
CC         ChEBI:CHEBI:175763; EC=4.2.3.60;
CC         Evidence={ECO:0000269|PubMed:22776156};
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:22776156};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.7 uM for farnesyl diphosphate {ECO:0000269|PubMed:22776156};
CC         Note=kcat is 0.01 sec(-1) with farnesyl diphosphate as substrate.;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in root.
CC       {ECO:0000269|PubMed:22776156}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; JQ437839; AFR42417.1; -; mRNA.
DR   AlphaFoldDB; J9RLZ7; -.
DR   SMR; J9RLZ7; -.
DR   GO; GO:0102904; F:germacrene C synthase activity; IEA:UniProtKB-EC.
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..563
FT                   /note="Germacrene C/D synthase"
FT                   /id="PRO_0000421725"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           315..319
FT                   /note="DDXXD motif"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         468
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   563 AA;  65455 MW;  D9FC2C0AAC5A983C CRC64;
     MESCLSVSSA PPPKKNIQEP VRPNANFHKS VWGDHFLKYA SNPEQINDGV DKQHKQLKEE
     LRKKLVVNVN IERAEEQLKL IDAIQRLGVA YHFRTEIASV LNNQLELWNN KVDDDDLYLT
     SLRFRLLRQQ GYNVSCAVFE KFKNIDGRFN ECLTDDVRGL LSLYESTHMR VHKEDILEEA
     LEFTVAQLEQ VIKSSLSDKV LLSQVVHALN IPIRKSLTRL EARYFISVYE QDKSCNETLL
     KFSKLDFNIL QKLHQQEVAD LTLWWKNLNV SEKVPYARDR LVECYFWALA EYFEPQYSRA
     RKMSGKITAL ISLIDDTYDS YGTFEELALF TDAAQRWDIN AIDQLPEYMR PIFRELIYLY
     NAMEEELLND GISYRVEYAK QSVIQMITAY NDEAIWYHNN YVPTFEEYLK VALVSSGYRM
     LPTNSFVGMG KTEVPHQAFD WVSNNPLMVK ASTIIARLDN DKVGHEHEQD RGHVASGVEC
     YMKQHGATKE EAVVEFNKRI SSAWKDINQE CLHPLPVPMH LLERVLNLVR FVTLFYKNGD
     MYTNSNTHMK EFISSLLVES IPS