ID   DGUS3_AQUCR             Reviewed;         547 AA.
AC   D0VMR8;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Delta-guaiene synthase 3;
DE            EC=4.2.3.87;
DE            EC=4.2.3.93;
GN   Name=C4;
OS   Aquilaria crassna (Eagle wood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Thymelaeaceae; Aquilaria.
OX   NCBI_TaxID=223751;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY METHYL JASMONATE.
RX   PubMed=20959422; DOI=10.1104/pp.110.161828;
RA   Kumeta Y., Ito M.;
RT   "Characterization of {delta}-Guaiene Synthases from Cultured Cells of
RT   Aquilaria, Responsible for the Formation of the Sesquiterpenes in
RT   Agarwood.";
RL   Plant Physiol. 154:1998-2007(2010).
CC   -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of delta-
CC       guaiene (78.2%) and alpha-guaiene (20.9%), two structures composed of
CC       five- and seven-membered rings. Produces also 0.9% of alpha-humulene.
CC       {ECO:0000269|PubMed:20959422}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = delta-guaiene + diphosphate;
CC         Xref=Rhea:RHEA:31831, ChEBI:CHEBI:33019, ChEBI:CHEBI:63447,
CC         ChEBI:CHEBI:175763; EC=4.2.3.93;
CC         Evidence={ECO:0000269|PubMed:20959422};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = alpha-guaiene + diphosphate;
CC         Xref=Rhea:RHEA:31807, ChEBI:CHEBI:33019, ChEBI:CHEBI:63443,
CC         ChEBI:CHEBI:175763; EC=4.2.3.87;
CC         Evidence={ECO:0000269|PubMed:20959422};
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=3.05 uM for farnesyl diphosphate {ECO:0000269|PubMed:20959422};
CC         Note=kcat is 7.34 x 10(-3) sec(-1) for farnesyl diphosphate.;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- INDUCTION: Up-regulated by methyl jasmonate.
CC       {ECO:0000269|PubMed:20959422}.
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. {ECO:0000305}.
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DR   EMBL; GU083699; ACY38197.1; -; mRNA.
DR   AlphaFoldDB; D0VMR8; -.
DR   SMR; D0VMR8; -.
DR   KEGG; ag:ACY38197; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0045338; P:farnesyl diphosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IDA:UniProtKB.
DR   GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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..547
FT                   /note="Delta-guaiene synthase 3"
FT                   /id="PRO_0000419797"
FT   MOTIF           299..303
FT                   /note="DDXXD motif"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
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         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   547 AA;  63943 MW;  4CA8749F86F3797D CRC64;
     MSSAKLGSAS EDVSRRDANY HPTVWGDFFL THSSDFLENN DSILEKHEEL KQEVRNLLVV
     ETSDLPSKIQ LTDDIIRLGV GYHFETEIKA QLEKLHDHQL HLNFDLLTTS VWFRLLRGHG
     FSISSDVFKR FKNTKGEFET EDARTLWCLY EATHLRVDGE DILEEAIQFS RKKLEALLPE
     LSFPLNECVR DALHIPYHRN VQRLAARQYI PQYDAEPTKI ESLSLFAKID FNMLQALHQR
     ELREASRWWK EFDFPSKLPY ARDRIAEGYY WMMGAHFEPK FSLSRKFLNR IIGITSLIDD
     TYDVYGTLEE VTLFTEAVER WDIEAVKDIP KYMQVIYIGM LGIFEDFKDN LINARGKDYC
     IDYAIEVFKE IVRSYQREAE YFHTGYVPSY DEYMENSIIS GGYKMFIILM LIGRGEFELK
     ETLDWASTIP EMVKASSLIA RYIDDLQTYK AEEERGETVS AVRCYMREYD VSEEEACKKM
     REMIEIEWKR LNKTTLEADE VSSSVVIPSL NFTRVLEVMY DKGDGYSDSQ GVTKDRIAAL
     LRHAIEI