ID   DCADS_STRCL             Reviewed;         327 AA.
AC   B5GS26;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=(-)-delta-cadinene synthase;
DE            EC=4.2.3.97;
GN   ORFNames=SCreLAV_p0328, SSCG_02150;
OS   Streptomyces clavuligerus.
OG   Plasmid pSCL4.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602; PLASMID=pSCL4;
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA   Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA   Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces clavuligerus ATCC 27064.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=21276937; DOI=10.1016/j.chembiol.2010.11.008;
RA   Hu Y., Chou W.K., Hopson R., Cane D.E.;
RT   "Genome mining in Streptomyces clavuligerus: expression and biochemical
RT   characterization of two new cryptic sesquiterpene synthases.";
RL   Chem. Biol. 18:32-37(2011).
CC   -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate into
CC       (-)-delta-cadinene. Cyclization mechanism involves an intermediate
CC       nerolidyl diphosphate leading to a helminthogermacradienyl cation.
CC       {ECO:0000269|PubMed:21276937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-delta-cadinene +
CC         diphosphate; Xref=Rhea:RHEA:32015, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:63703, ChEBI:CHEBI:175763; EC=4.2.3.97;
CC         Evidence={ECO:0000269|PubMed:21276937};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.4 uM for (2E,6E)-farnesyl diphosphate
CC         {ECO:0000269|PubMed:21276937};
CC         Note=kcat is 0.00114 sec(-1).;
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; CM000914; EFG03819.2; -; Genomic_DNA.
DR   EMBL; DS570637; EDY49122.1; -; Genomic_DNA.
DR   RefSeq; WP_003954606.1; NZ_CP027859.1.
DR   AlphaFoldDB; B5GS26; -.
DR   SMR; B5GS26; -.
DR   STRING; 443255.SCLAV_p0328; -.
DR   EnsemblBacteria; EDY49122; EDY49122; SSCG_02150.
DR   KEGG; ag:EFG03819; -.
DR   eggNOG; ENOG502Z881; Bacteria.
DR   OMA; DLIEYAM; -.
DR   OrthoDB; 1869158at2; -.
DR   BRENDA; 4.2.3.97; 5988.
DR   Proteomes; UP000002357; Plasmid pSCL4.
DR   Proteomes; UP000006569; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Lyase; Magnesium; Metal-binding; Plasmid; Reference proteome.
FT   CHAIN           1..327
FT                   /note="(-)-delta-cadinene synthase"
FT                   /id="PRO_0000418477"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  35838 MW;  471B84889442CF01 CRC64;
     MSTRPVEGSA IWDVLSPHSP HAAAADGKTL VWVEAGELCG HDTAESANLA RIRPGLLAAF
     CHPKATEDDL TLITKWMAWL FLLDDRIDES DLGRDADLLD GHLQDLQGVA LGIRTASGPM
     SRALEEIITQ ASAGMGDAWQ LRFRRNISDY LLACVWQAAH RQAGEFPDPE VFPHWRRAFG
     AIMPSFDLIE RTDGGALPSC VYYSRPYQSL LTAAADLVCW TNDLMTVDKE AAHGDLHNLV
     LVTEHDRHQD RRTASAAVSA ACEQRMRAHT SARRDLTGLT AALGLPDTVR THADDCAASL
     LVWVRGHLEW GLETPRYRPG TTGTGTD