DCS1_GOSHI
ID DCS1_GOSHI Reviewed; 554 AA.
AC P93665;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=(+)-delta-cadinene synthase;
DE Short=D-cadinene synthase;
DE EC=4.2.3.13;
GN Name=CDN1;
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Westburn M;
RA Davis E.M., Chen Y.-S., Essenberg M., Pierce M.L.;
RT "cDNA sequence of a (+)-delta-cadinene synthase gene induced in Gossypium
RT hirsutum L. by bacterial infection.";
RL (er) Plant Gene Register PGR98-040(1998).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=8728715; DOI=10.1016/0031-9422(95)00771-7;
RA Davis E.M., Tsuji J., Davis G.D., Pierce M.L., Essenberg M.;
RT "Purification of (+)-delta-cadinene synthase, a sesquiterpene cyclase from
RT bacteria-inoculated cotton foliar tissue.";
RL Phytochemistry 41:1047-1055(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 -!- INDUCTION: By bacterial infection.
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}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Delta-cadinene synthase entry;
CC URL="https://en.wikipedia.org/wiki/Delta-cadinene_synthase";
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DR EMBL; U88318; AAC12784.1; -; mRNA.
DR RefSeq; NP_001313854.1; NM_001326925.1.
DR AlphaFoldDB; P93665; -.
DR SMR; P93665; -.
DR PRIDE; P93665; -.
DR GeneID; 107903500; -.
DR KEGG; ag:AAC12784; -.
DR KEGG; ghi:107903500; -.
DR BRENDA; 4.2.3.13; 2499.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000189702; Genome assembly.
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:AgBase.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; 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 Direct protein sequencing; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..554
FT /note="(+)-delta-cadinene synthase"
FT /id="PRO_0000186443"
FT REGION 1..23
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; 64020 MW; 8BCC78AD8CA5B816 CRC64;
MASQVSQMPS SSPLSSNKDE MRPKADFQPS IWGDFFLNCP DKNIDAETQK RHQQLKEEVR
KMIVAPMANS TLKLAFIDSV QGLGVSYHFT KEIEDELENI YHNNNDAEND LYTTSLRFRL
LREHGFHVSC DVFNKFKDEQ GNFKSSVTSD VRGLLELYQA SYLRVHGEDI LDEAISFTSN
HLSLAVASLD HPLSEEVSHA LKQSIRRGLP RVEARHYLSV YQDIESHNKV LLEFAKIDFN
MVQLLHRKEL SEISRWWKDL DFQRKLPYAR DRVVEGYFWI SGVYFEPQYS LGRKMLTKVI
AMASIVDDTY DSYATYEELI PYTNAIERWD IKCIDELPEY MKPSYKALLD VYEEMEQLVA
EHGRQYRVEY AKNAMIRLAQ SYLVEARWTL QNYKPSFEEF KANALPTCGY AMLAITSFVG
MGDIVTPETF KWAANDPKII QASTIICRFM DDVTEHKFKH RREDDCSAIE CYMEEYGVTA
QEAYDVFNKH VESAWKDVNQ GFLKPTEMPT EVLNRSLNLA RVMDVLYREG DGYTYVGKAA
KGGITSLLIE PIAL
