GCSY1_CUCME
ID GCSY1_CUCME Reviewed; 571 AA.
AC B2KSJ5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=(+)-gamma-cadinene synthase;
DE Short=CmTpsNY;
DE EC=4.2.3.13;
DE EC=4.2.3.92;
DE AltName: Full=(+)-delta-cadinene synthase;
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Noy Yizre'el;
RX PubMed=18264780; DOI=10.1007/s11103-008-9296-6;
RA Portnoy V., Benyamini Y., Bar E., Harel-Beja R., Gepstein S.,
RA Giovannoni J.J., Schaffer A.A., Burger J., Tadmor Y., Lewinsohn E.,
RA Katzir N.;
RT "The molecular and biochemical basis for varietal variation in
RT sesquiterpene content in melon (Cucumis melo L.) rinds.";
RL Plant Mol. Biol. 66:647-661(2008).
CC -!- FUNCTION: Sesquiterpene synthase producing mainly delta- and gamma-
CC cadinene with traces of several other sesquiterpenoids, including
CC alpha-copaene. Associated with the production of sesquiterpenes
CC responsible for the aroma of the fruit. {ECO:0000269|PubMed:18264780}.
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:18264780};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,8aR)-delta-cadinene +
CC diphosphate; Xref=Rhea:RHEA:19525, ChEBI:CHEBI:15385,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.13;
CC Evidence={ECO:0000269|PubMed:18264780};
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the rind tissues of ripe fruits.
CC {ECO:0000269|PubMed:18264780}.
CC -!- DEVELOPMENTAL STAGE: Expressed during ripening.
CC {ECO:0000269|PubMed:18264780}.
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. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; EU158098; ABX83200.1; -; mRNA.
DR RefSeq; NP_001284382.1; NM_001297453.1.
DR AlphaFoldDB; B2KSJ5; -.
DR SMR; B2KSJ5; -.
DR GeneID; 103493386; -.
DR KEGG; cmo:103493386; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR OrthoDB; 360509at2759; -.
DR BRENDA; 4.2.3.46; 1735.
DR BRENDA; 4.2.3.62; 1735.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047461; F:(+)-delta-cadinene synthase activity; IEA:UniProtKB-EC.
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: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 Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..571
FT /note="(+)-gamma-cadinene synthase"
FT /id="PRO_0000419798"
FT MOTIF 323..327
FT /note="DDXXD motif"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 571 AA; 66633 MW; 5F6D1370E817D409 CRC64;
MSSQVSNFPA SIMKTNDIPD VKRSLANFHP NIWKEHFLSF TFDDALKIDE GMKERTEKLK
EEIRMMMIAY VENQLIKLNL VDSIQRLGVS YHFEDEVDEF LEHIYVSYNN SLLLSNKNSN
GEDLHITALL FRLLRQQGYR ISCDIFLKFM DDNGKFKESL VEDERGLLSL YEASHMMGHG
EALLEEALEF TTTHLQTYIH RYSNINPSFA SEVSNALKLP IRKSVPRIKA REYLEIYQQH
PSHNETLLEF SKLDFNILQK LHQKELSEIC RWWKDLDVPT KFPFARDRIV ECYFWTLGAY
FEPQYSVGRK MLTKVIAIAS ILDDIYDAYG TFEELQVLTP AIQRWDRSMV HTLPLYMKPF
YVAMLELYEE IGKEIDKDQN SLHLQVAIGG IKRLSESYFE EAKWLNKEYK PSFKEYMELA
LKTTGYTMLI SISFLGLGDH IVTNEVLQWL SNGPQIIKAS TIICRLMDDI ASHKFEQERE
HVASAVECYM KQYDCSEEEA CIELHKEVVD AWKDTNEAFY RPFNVPVPVL MRVLNFSRVI
NLLYLDEDGY TNAKSGTKFL IKSLLVDPLP C
