ID   GCS1_OCIBA              Reviewed;         540 AA.
AC   Q5SBP5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Gamma-cadinene synthase;
DE            EC=4.2.3.92;
DE   AltName: Full=(+)-gamma-cadinene synthase;
GN   Name=CDS;
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 cyclization of
CC       trans,trans-farnesyl diphosphate (FPP) to gamma cadinene.
CC       {ECO:0000269|PubMed:15516500}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (+)-gamma-cadinene +
CC         diphosphate; Xref=Rhea:RHEA:31827, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:63205, ChEBI:CHEBI:175763; EC=4.2.3.92;
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}.
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DR   EMBL; AY693645; AAV63787.1; -; mRNA.
DR   AlphaFoldDB; Q5SBP5; -.
DR   SMR; Q5SBP5; -.
DR   KEGG; ag:AAV63787; -.
DR   UniPathway; UPA00213; -.
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   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..540
FT                   /note="Gamma-cadinene synthase"
FT                   /id="PRO_0000399250"
FT   MOTIF           292..296
FT                   /note="DDXXD motif"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         436
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  63566 MW;  F1B44726BF7A2B97 CRC64;
     MDVSILRDVR PPVTSYAPNI WADTFSNISL DEEVQKKYAE TIEALKQVVR GMLMAAATPI
     KQMIFIDTLE RLGLAYHFET EIEHKLQKIY DDNVCGDDCD LFTTALRFRL LRQHRHHVSC
     DVFDKFLYEE GKFKGDAEGL LSLYEASHVR FHNEKILEEA ERFTRQELSC WIKLQSPLKD
     KVKRALERPL HREVPILYAR HFISIYEKDE SMDEHLLKLA KFNFNFLQNL YKKELYDLSR
     WWNKFDLKTK LPYIRDRLAE AYLWGVGYHF EPQYSYVRKG VVLSIKIIGI LDDTYDNYAT
     VNEAQLFTEI LDRWSMDEID RLPDYMKIVL HFVMSAYEEY ERDAKIVYGK KFASPYFKET
     IQQLARGYNQ ELKWVMEKQM PPFKDYLKNS EITSCIYIMF ASIIPGLKSF TQEAIDWIKN
     EPNFAVKAGL IGRYWDDIGS HKRESKGGEM LTVMDCYMKQ YSVSIQETIS EFAKAVEDSW
     KEVNEGWVYT ISMSKEITVQ FLNYSRMCDA SYNRNNGDGY TDPSFAKSNI TALFVDPIII