DGUSI_AQUCR
ID DGUSI_AQUCR Reviewed; 547 AA.
AC D0VMR5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Inactive delta-guaiene synthase;
GN Name=C1;
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], INDUCTION BY METHYL JASMONATE, MUTAGENESIS OF
RP TYR-110; TRP-144; VAL-241; PRO-296 AND HIS-337, AND 3D-STRUCTURE MODELING.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
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 -!- MISCELLANEOUS: Site-directed mutagenesis and 3-D homology modeling
CC suggest that the structure of the N-terminal domain is important in
CC facilitating proper folding of the protein to form a catalytically
CC active enzyme. {ECO:0000305|PubMed:20959422}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; GU083696; ACY38194.1; -; mRNA.
DR AlphaFoldDB; D0VMR5; -.
DR SMR; D0VMR5; -.
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 Magnesium; Metal-binding.
FT CHAIN 1..547
FT /note="Inactive delta-guaiene synthase"
FT /id="PRO_0000419794"
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"
FT MUTAGEN 110
FT /note="Y->S: Restore guaiene synthase activity; when
FT associated with E-241; S-296 and Y-337. Restore guaiene
FT synthase activity; when associated with R-144; E-241; S-296
FT and Y-337. No effect; when associated with R-144; S-296 and
FT Y-337. No effect; when associated with R-144; E-241 and Y-
FT 337. No effect; when associated with R-144; E-241 and S-
FT 296."
FT /evidence="ECO:0000269|PubMed:20959422"
FT MUTAGEN 144
FT /note="W->R: Restore guaiene synthase activity; when
FT associated with Y-110; E-241; S-296 and Y-337. No effect;
FT when associated with E-241; S-296 and Y-337. No effect;
FT when associated with Y-110; S-296 and Y-337. No effect;
FT when associated with Y-110; E-241 and Y-337. No effect;
FT when associated with Y-110; E-241 and S-296."
FT /evidence="ECO:0000269|PubMed:20959422"
FT MUTAGEN 241
FT /note="V->E: Restore guaiene synthase activity; when
FT associated with Y-110; S-296 and Y-337. Restore guaiene
FT synthase activity; when associated with Y-110; R-144; S-296
FT and Y-337. No effect; when associated with R-144; S-296 and
FT Y-337. No effect; when associated with Y-110; R-144 and Y-
FT 337. No effect; when associated with Y-110; R-144 and S-
FT 296."
FT /evidence="ECO:0000269|PubMed:20959422"
FT MUTAGEN 296
FT /note="P->S: Restore guaiene synthase activity; when
FT associated with Y-110; E-241 and Y-337. Restore guaiene
FT synthase activity; when associated with Y-110; R-144; E-241
FT and Y-337. No effect; when associated with R-144; E-241 and
FT Y-337. No effect; when associated with Y-110; R-144 and Y-
FT 337. No effect; when associated with Y-110; R-144 and E-
FT 241."
FT /evidence="ECO:0000269|PubMed:20959422"
FT MUTAGEN 337
FT /note="H->Y: Restore guaiene synthase activity; when
FT associated with Y-110; E-241 and S-296. Restore guaiene
FT synthase activity; when associated with Y-110; R-144; E-241
FT and S-296. No effect; when associated with R-144; E-241 and
FT S-296. No effect; when associated with Y-110; R-144 and S-
FT 296. No effect; when associated with Y-110; R-144 and E-
FT 241."
FT /evidence="ECO:0000269|PubMed:20959422"
SQ SEQUENCE 547 AA; 63874 MW; 5E3235B8661B8EF9 CRC64;
MSSAKLGSAS EDVSRRDANY HPTVWGDFFL THSSNFLENN DSILEKHEEL KQEVRNLLVV
ETSDLPSKIQ LTDEIIRLGV GYHFETEIKA QLEKLHDHQL HLNFDLLTTY VWFRLLRGHG
FSISSDVFKR FKNTKGEFET EDAWTLWCLY EATHLRVDGE DILEEAIQFS RKKLEALLPE
LSFPLNECVR DALHIPYHRN VQRLAARQYI PQYDAEPTKI ESLSLFAKID FNMLQALHQS
VLREASRWWK EFDFPSKLPY ARDRIAEGYY WMMGAHFEPK FSLSRKFLNR IIGITPLIDD
TYDVYGTLEE VTLFTEAVER WDIEAVKDIP KYMQVIHTGM LGIFEDFKDN LINARGKDYC
IDYAIEVFKE IVRSYQREAE YFHTGYVPSY DEYMENSIIS GGYKMFIILM LIGRGEFELK
ETLDWASTIP EMVKASSLIA RYIDDLQTYK AEEERGETVS AVRCYMREFG VSEEQACKKM
REMIEIEWKR LNKTTLEADE ISSSVVIPSL NFTRVLEVMY DKGDGYSDSQ GVTKDRIAAL
LRHAIEI
