ID   DCS4_GOSAR              Reviewed;         554 AA.
AC   O49853;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=(+)-delta-cadinene synthase isozyme C2;
DE            Short=D-cadinene synthase C2;
DE            EC=4.2.3.13;
GN   Name=CAD1-C2;
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;
RA   Meng Y., Jia J., Liu C., Liang W., Zhou X., Heinstein P., Chen X.-Y.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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; Y16432; CAA76223.1; -; mRNA.
DR   RefSeq; NP_001316934.1; NM_001330005.1.
DR   AlphaFoldDB; O49853; -.
DR   SMR; O49853; -.
DR   GeneID; 108449980; -.
DR   BRENDA; 4.2.3.13; 2497.
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: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   2: Evidence at transcript level;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..554
FT                   /note="(+)-delta-cadinene synthase isozyme C2"
FT                   /id="PRO_0000186442"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           307..311
FT                   /note="DDXXD motif"
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"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         455
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  64118 MW;  35DDD66D3E838AAC CRC64;
     MASQVSQMPS SSPLSSNKDE IRPKADFQPS IWGDFFLNCP DKNIDAGTEK RHQQLKEEVR
     KMIVAPMANS TQKLAFIDSV QRLGVSYHFT KEIEDELENI YHNNNDAEND LYTTSLRFRL
     LREHGYNVSC DVFNKFKDEQ GNFKSSVTSD VQGLLELYQA SYLRVHGEDI LDEAISFTTN
     HLSLAVSSLD HPLSEEVSHA LKQSIRRGLP RVEARHYLSV YQDIESHNKA LLEFAKIDFN
     MLQFLHRKEL SEICRWWKDL DFQRKLPYAR DRVVEGYFWI SGVYFEPQYS LGRKMLTKVI
     AMASIVDDTY DSYATYEELI PYTNAIERWD IKCIDELPEY MKPSYKALLD VYKEMEQLVA
     EHGRQYRVEY AKNAMIRLAQ SYLVEARWTL QNYKPSFEEF KANALPTCGY AMLAITSFVG
     MGDIVTPETF KWAANDPKII QASTIICRFM DDVAEHKFKH RREDDCSAIE CYMEEYGVSA
     QEAYDVFNKH VESAWKDVNQ EFQKPTEMPT EVLNRSLNLA RVMDVLYREG DGYTYVGKAA
     KGGITSLLIE PIAL