DCS3_GOSAR
ID DCS3_GOSAR Reviewed; 555 AA.
AC Q43714;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=(+)-delta-cadinene synthase isozyme A;
DE Short=D-cadinene synthase A;
DE EC=4.2.3.13;
GN Name=CAD1-A;
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nanking;
RX PubMed=8904844; DOI=10.1021/np960344w;
RA Chen X.-Y., Wang M., Chen Y., Davisson V.J., Heinstein P.;
RT "Cloning and heterologous expression of a second (+)-delta-cadinene
RT synthase from Gossypium arboreum.";
RL J. Nat. Prod. 59:944-951(1996).
CC -!- FUNCTION: Responsible for the cyclization of trans,trans-farnesyl
CC diphosphate (FPP) to (+)-delta cadinene.
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 -!- 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 -!- 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; X96429; CAA65289.1; -; mRNA.
DR EMBL; U27535; AAB41259.1; -; mRNA.
DR RefSeq; NP_001316949.1; NM_001330020.1.
DR AlphaFoldDB; Q43714; -.
DR SMR; Q43714; -.
DR GeneID; 108463032; -.
DR UniPathway; UPA00213; -.
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:0048653; P:anther development; IEP:AgBase.
DR GO; GO:0048825; P:cotyledon development; IEP:AgBase.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0090377; P:seed trichome initiation; TAS:AgBase.
DR GO; GO:0048442; P:sepal development; IEP:AgBase.
DR GO; GO:0048480; P:stigma development; IEP:AgBase.
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; 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 SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..555
FT /note="(+)-delta-cadinene synthase isozyme A"
FT /id="PRO_0000186441"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 308..312
FT /note="DDXXD motif"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 555 AA; 64104 MW; 7060C4F9D99412F9 CRC64;
MASQASQVLA SPHPAISSEN RPKADFHPGI WGDMFIICPD TDIDAATELQ YEELKAQVRK
MIMEPVDDSN QKLPFIDAVQ RLGVSYHFEK EIEDELENIY RDTNNNDADT DLYTTALRFR
LLREHGFDIS CDAFNKFKDE AGNFKASLTS DVQGLLELYE ASYMRVHGED ILDEAISFTT
AQLTLALPTL HHPLSEQVGH ALKQSIRRGL PRVEARNFIS IYQDLESHNK SLLQFAKIDF
NLLQLLHRKE LSEICRWWKD LDFTRKLPFA RDRVVEGYFW IMGVYFEPQY SLGRKMLTKV
IAMASIVDDT YDSYATYDEL IPYTNAIERW DIKCMNQLPN YMKISYKALL NVYEEMEQLL
ANQGRQYRVE YAKKAMIRLV QAYLLEAKWT HQNYKPTFEE FRDNALPTSG YAMLAITAFV
GMGEVITPET FKWAASDPKI IKASTIICRF MDDIAEHKFN HRREDDCSAI ECYMKQYGVT
AQEAYNEFNK HIESSWKDVN EEFLKPTEMP TPVLCRSLNL ARVMDVLYRE GDGYTHVGKA
AKGGITSLLI DPIQI
