DGUS2_AQUCR
ID DGUS2_AQUCR Reviewed; 547 AA.
AC D0VMR7;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Delta-guaiene synthase 2;
DE EC=4.2.3.87;
DE EC=4.2.3.93;
GN Name=C3;
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 (53.7%) and alpha-guaiene (44.6%), two structures composed of
CC five- and seven-membered rings. Produces also 1.7% 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=0.51 uM for farnesyl diphosphate {ECO:0000269|PubMed:20959422};
CC Note=kcat is 9.72 x 10(-5) 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; GU083698; ACY38196.1; -; mRNA.
DR AlphaFoldDB; D0VMR7; -.
DR SMR; D0VMR7; -.
DR KEGG; ag:ACY38196; -.
DR BioCyc; MetaCyc:MON-16040; -.
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 2"
FT /id="PRO_0000419796"
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; 63853 MW; 962BBCE10A89EB3A CRC64;
MSSAKLGSAS EDVSRRDANY HPTVWGDFFL THSSNFLENN DSILEKHEEL KQEVRNLLVV
ETSDLPSKIQ LTDEIIRLGV GYHFETEIKA QLEKLHDHQL HLNFDLLTTS VWFRLLRGHG
FSIPSDVFKR FKNTKGEFET EDARTLWCLY EATHLRVDGE DILEEAIQFS RKRLEALLPK
LSFPLSECVR DALHIPYHRN VQRLAARQYI PQYDAEQTKI ESLSLFAKID FNMLQALHQS
ELREASRWWK EFDFPSKLPY ARDRIAEGYY WMMGAHFEPK FSLSRKFLNR IVGITSLIDD
TYDVYGTLEE VTLFTEAVER WDIEAVKDIP KYMQVIYIGM LGIFEDFKDN LINARGKDYC
IDYAIEVFKE IVRSYQREAE YFHTGYVPSY DEYMENSIIS GGYKMFIILM LIGRGEFELK
ETLDWASTIP EMVKASSLIA RYIDDLQTYK AEEERGETVS AVRCYMREFG VSEEQACKKM
REMIEIEWKR LNKTTLEADE ISSSVVIPSL NFTRVLEVMY DKGDGYSDSQ GVTKDRIAAL
LRHAIEI
