ID   DCS2_GOSAR              Reviewed;         554 AA.
AC   Q39760;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=(+)-delta-cadinene synthase isozyme XC14 {ECO:0000303|PubMed:8554317};
DE            Short=D-cadinene synthase XC14 {ECO:0000305};
DE            EC=4.2.3.13 {ECO:0000269|PubMed:8554317};
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], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Nanking;
RX   PubMed=8554317; DOI=10.1006/abbi.1995.0038;
RA   Chen X.-Y., Chen Y., Heinstein P., Davisson V.J.;
RT   "Cloning, expression, and characterization of (+)-delta-cadinene synthase:
RT   a catalyst for cotton phytoalexin biosynthesis.";
RL   Arch. Biochem. Biophys. 324:255-266(1995).
CC   -!- FUNCTION: Responsible for the cyclization of trans,trans-farnesyl
CC       diphosphate (FPP) to (+)-delta cadinene. {ECO:0000269|PubMed:8554317}.
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:8554317};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19526;
CC         Evidence={ECO:0000269|PubMed:8554317};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8554317};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305}.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; U23205; AAA93065.1; -; mRNA.
DR   PIR; S68366; S68366.
DR   RefSeq; NP_001316936.1; NM_001330007.1.
DR   AlphaFoldDB; Q39760; -.
DR   SMR; Q39760; -.
DR   GeneID; 108450450; -.
DR   KEGG; ag:AAA93065; -.
DR   BRENDA; 4.2.3.13; 2497.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0047461; F:(+)-delta-cadinene synthase activity; IDA:AgBase.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009620; P:response to fungus; IDA: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   1: Evidence at protein level;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..554
FT                   /note="(+)-delta-cadinene synthase isozyme XC14"
FT                   /id="PRO_0000186440"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           307..311
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   554 AA;  64159 MW;  A88974665E0F6B2B CRC64;
     MASQVSQMPS SSPLSSNKDE MRPKADFQPS IWGDLFLNCP DKNIDAETEK RHQQLKEEVR
     KMIVAPMANS TQKLAFIDSV QRLGVSYHFT KEIEDELENI YHNNNDAEND LYTTSLRFRL
     LREHGFNVSC DVFNKFKDEQ GNFKSSVTSD VRGLLELYQA SYLRVHGEDI LDEAISFTTN
     HLSLAVASLD YPLSEEVSHA LKQSIRRGLP RVEARHYLSV YQDIESHNKV LLEFAKIDFN
     MVQLLHRKEL SEISRWWKDL DFQRKLPYAR DRVVEGYFWI SGVYFEPQYS LGRKMLTKVI
     AMASIVDDTY DSYATYEELI PYTKAIERWD IKCIDELPEY MKPSYKALLD VYEEMEQLVA
     KHGRQYRVEY AKNAMIRLAQ SYLVEARWTL QNYKPSFEEF KANALPTCGY AMLAITSFVG
     MGDIVTPETF KWAANDPKII QASTIICRFM DDVAEHKFKH RREDDCSAIE CYMEEYGVTA
     QEAYDVFNKH VESAWKDVNK EFLKPTEMPT EVLNRSLNLA RVMDVLYREG DGYTYVGKAA
     KGGITSLLIE PVAL