CAD_CHAFM
ID CAD_CHAFM Reviewed; 603 AA.
AC I1ZHA5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Sesquiterpene synthase Cad {ECO:0000303|Ref.1};
DE AltName: Full=Beta-cadinene synthase {ECO:0000303|Ref.1};
DE Short=Cf-Cad {ECO:0000303|Ref.1};
DE EC=4.2.3.- {ECO:0000269|Ref.1};
GN Name=CAD {ECO:0000303|Ref.1};
OS Chamaecyparis formosensis (Formosan cypress) (Cupressus formosensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Chamaecyparis.
OX NCBI_TaxID=187461;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX DOI=10.1515/hf-2011-0224;
RA Kuo P.-M., Hsu K.-H., Lee Y.-R., Chu F.-H., Wang S.-Y.;
RT "Isolation and characterization of beta-cadinene synthase cDNA from
RT Chamaecyparis formosensis Matsum.";
RL Holzforschung 66:569-576(2012).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds (Ref.1). Mediates the conversion of (2E,6E)-farnesyl
CC diphosphate (FPP) into beta-cadinene (Ref.1). Not active with geranyl
CC diphosphate (GPP) and geranylgeranyl diphosphate (GGPP) as substrates
CC (Ref.1). {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-cadinene + diphosphate;
CC Xref=Rhea:RHEA:68596, ChEBI:CHEBI:27723, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68597;
CC Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and, to a lower extent,
CC in stems and xylem. {ECO:0000269|Ref.1}.
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 {ECO:0000250|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; JN715077; AFJ23663.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:1901928; P:cadinene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..603
FT /note="Sesquiterpene synthase Cad"
FT /id="PRO_0000454949"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 357..361
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 603 AA; 70796 MW; 98C919CE6513C301 CRC64;
MAEVGLSQNS YASANHDKKS EQQIRRRVAE FHPNVWEYEF LQSLSSPYGA PSYCERINIL
IEEIKMDIFD GLVGDGEKNM NPSAYDLLER FFVVDILQSL GIERHFKKEI KAVLDYTYKY
WNDEKGISLA SGNLIVDLNT NALGFKVLRL NEYYVSPDVF QNFQDEMGQF IDLENFKEDE
SKLRSLLSLY RASEICFPEE NILKQAKMFA STCLRQAIEE NRELVNKSQL IIEVEYIMKY
PWTCRVPRWE VWNYIKIFRG DTDASMCMKG VYEMPSDKRT KILELAILDF NILQDQHHNE
LKILSKWWNE TKVKELNFFR QRHVEFYFLY ACGLYEKELS ATRLCFAKVG ALITLLDDIF
DTYGTIDELV PFATALIKWD MSIMNHLPEY MKTCFQFAYK TYMEIATEAE KIHGPCVQKW
MHDTWKTIIL AQLQDAEWIA NNYLPSLTEY LESSVPSTTV PVLSLFSMLL IDTIFPDDII
EKITKFQSCV AWGCRLVDDS KDFQDEKEHG ESASWIECYM KENPGTTRKQ ALDHANMLIE
SNFEELIKHR IFYEYCIPST CKRLYFDMYR SVAFIFKDID GFSKSSKAIR DDIKKILVEP
IYF
