ID   TPS2_VALOF              Reviewed;         562 AA.
AC   J9R5V4;
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=Valerena-4,7(11)-diene synthase;
DE            EC=4.2.3.139;
DE   AltName: Full=Terpene synthase 2;
DE            Short=VoTPS2;
GN   Name=TPS2;
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: Catalyzes formation of valerena-4,7(11)-diene, one of the
CC       active ingredients responsible for the sedative effect extracted from
CC       Valeriana officinalis root. {ECO:0000269|PubMed:22776156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + valerena-4,7(11)-
CC         diene; Xref=Rhea:RHEA:34467, ChEBI:CHEBI:33019, ChEBI:CHEBI:68625,
CC         ChEBI:CHEBI:175763; EC=4.2.3.139;
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=9.5 uM for farnesyl diphosphate {ECO:0000269|PubMed:22776156};
CC         Note=kcat is 0.013 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; JQ437840; AFR42418.1; -; mRNA.
DR   AlphaFoldDB; J9R5V4; -.
DR   SMR; J9R5V4; -.
DR   KEGG; ag:AFR42418; -.
DR   BioCyc; MetaCyc:MON-17911; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0102412; F:valerena-4,7(11)-diene synthase activity; IEA:UniProtKB-EC.
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..562
FT                   /note="Valerena-4,7(11)-diene synthase"
FT                   /id="PRO_0000421726"
FT   MOTIF           314..318
FT                   /note="DDXXD motif"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   562 AA;  65880 MW;  746BE2119E4FD731 CRC64;
     MESCLSFSSP PPTKKNIQEP VRPNAKFHKS VWGNHFLKYA SNPEQIDYDA DEQHEQLKEE
     LRKKLVVNVT NERVEEQLKL IDAIQRLGVA YHFQREIDAV LNNLLLFRSN KDSDDIYMVS
     LRFRLLRQQG HNVSCSVFEK FKNIDGRFKD SLRDDVRGLL SLYEATHMRV HKEDILEEAL
     EFTIYELEQV VKLSSNDTLL ASEVIHALNM PIRKGLTRIE ARHFISVYQH DKSHDETLLK
     FSKIDFNMLQ KLHQRELADL TIWWEKLNVA EKMPYARDRF VECYFWGLGV YFEPQYSRAR
     KMFVKVINLT SLIDDTYDSY GTFDELDLFT DAVKRWNVNE TDKLPEYMRP LFMELLNVYN
     AMEEELKEEG VSYRVEYAKQ SMIQIVTAYN DEAIWYHNGY VPTFDEYLKV ALISCGYMLL
     STISFVGMGV TTVTKPAFDW VTNNPLILIA SCTINRLADD KVGHELEQER GHVASGVECY
     MKHNNATKQE VVIEFNKRIS NAWKDINQEC LHPLPVPLHL VVRPLYLACF MNVFYKDEDW
     YTHSNTQMKE CINSLLVESV PY