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 24-JAN-2024, entry version 112. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U88318; AAC12784.1; -; mRNA. DR RefSeq; NP_001313854.1; NM_001326925.1. DR AlphaFoldDB; P93665; -. DR SMR; P93665; -. DR STRING; 3635.P93665; -. DR PaxDb; 3635-P93665; -. DR GeneID; 107903500; -. DR KEGG; ag:AAC12784; -. DR KEGG; ghi:107903500; -. DR OrthoDB; 1209509at2759; -. 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; Farnesyl Diphosphate Synthase; 1. DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 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 PANTHER; PTHR31225:SF215; (+)-DELTA-CADINENE SYNTHASE; 1. DR PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01604; Terpene_Cyclase_Like_1_C_Termi; 1. DR SFLD; SFLDG01014; Terpene_Cyclase_Like_1_N-term; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 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 //