DCS1_GOSAR
ID DCS1_GOSAR Reviewed; 554 AA.
AC Q39761;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=(+)-delta-cadinene synthase isozyme XC1;
DE Short=D-cadinene synthase XC1;
DE EC=4.2.3.13;
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;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF
RP ASP-307; ASP-311; ASP-451; ASP-452 AND GLU-455.
RX PubMed=19489610; DOI=10.1021/bi900483b;
RA Gennadios H.A., Gonzalez V., Di Costanzo L., Li A., Yu F., Miller D.J.,
RA Allemann R.K., Christianson D.W.;
RT "Crystal structure of (+)-delta-cadinene synthase from Gossypium arboreum
RT and evolutionary divergence of metal binding motifs for catalysis.";
RL Biochemistry 48:6175-6183(2009).
CC -!- FUNCTION: Responsible for the cyclization of trans,trans-farnesyl
CC diphosphate (FPP) to (+)-delta cadinene. {ECO:0000269|PubMed:19489610}.
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:19489610};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19489610};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:19489610};
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; U23206; AAA93064.1; -; mRNA.
DR PIR; S68365; S68365.
DR PDB; 3G4D; X-ray; 2.40 A; A/B=1-554.
DR PDB; 3G4F; X-ray; 2.65 A; A/B=1-554.
DR PDBsum; 3G4D; -.
DR PDBsum; 3G4F; -.
DR AlphaFoldDB; Q39761; -.
DR SMR; Q39761; -.
DR PRIDE; Q39761; -.
DR KEGG; ag:AAA93064; -.
DR BRENDA; 4.2.3.13; 2497.
DR UniPathway; UPA00213; -.
DR EvolutionaryTrace; Q39761; -.
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; 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 3D-structure; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..554
FT /note="(+)-delta-cadinene synthase isozyme XC1"
FT /id="PRO_0000186439"
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 BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT MUTAGEN 307
FT /note="D->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:19489610"
FT MUTAGEN 308
FT /note="D->A: Reduces affinity for substrate about 12-fold."
FT MUTAGEN 311
FT /note="D->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:19489610"
FT MUTAGEN 451
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:19489610"
FT MUTAGEN 452
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:19489610"
FT MUTAGEN 455
FT /note="E->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:19489610"
FT TURN 31..37
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 46..64
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:3G4D"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3G4F"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:3G4D"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 229..260
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 290..310
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 342..359
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 366..390
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 410..419
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 438..456
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 480..502
FT /evidence="ECO:0007829|PDB:3G4D"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 510..526
FT /evidence="ECO:0007829|PDB:3G4D"
FT HELIX 538..548
FT /evidence="ECO:0007829|PDB:3G4D"
SQ SEQUENCE 554 AA; 64138 MW; 59D6922DEDF9DCAF CRC64;
MASQVSQMPS SSPLSSNKDE MRPKADFQPS IWGDLFLNCP DKNIDAETEK RHQQLKEEVR
KMIVAPMANS TQKLAFIDSV QRLGVSYHFT KEIEDELENI YHNNNDAEND LYTTSIRFRL
LREHGYNVSC DVFNKFKDEQ GNFKSSVTSD VRGLLELYQA SYLRVHGEDI LDEAISFTTH
HLSLAVASLD HPLSEEVSHA LKQSIRRGLP RVEARHYLSV YQDIESHNKA LLEFAKIDFN
MLQFLHRKEL SEICRWWKDL DFQRKLPYAR DRVVEGYFWI SGVYFEPQYS LGRKMLTKVI
AMASIVDDTY DSYATYEELI PYTNAIERWD IKCIDEIPEY MKPSYKALLD VYEEMVQLVA
EHGRQYRVEY AKNAMIRLAQ SYLVEAKWTL QNYKPSFEEF KANALPTCGY AMLAITSFVG
MGDIVTPETF KWAASDPKII QASTIICRFM DDVAEHKFKH RREDDCSAIE CYMEEYGVTA
QEAYDVFNKH VESAWKDLNQ EFLKPTEMPT EVLNRSLNLA RVMDVLYREG DGYTYVGKAA
KGGITSLLIE PIAL
