TS23M_MAIZE
ID TS23M_MAIZE Reviewed; 547 AA.
AC A0A3L6G998;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=(E)-beta-caryophyllene synthase {ECO:0000250|UniProtKB:B2C4D0};
DE EC=4.2.3.57 {ECO:0000250|UniProtKB:B2C4D0};
DE AltName: Full=Terpene synthase 23 {ECO:0000250|UniProtKB:B2C4D0};
GN Name=TPS23 {ECO:0000250|UniProtKB:B2C4D0};
GN ORFNames=Zm00014a_002860 {ECO:0000312|EMBL:PWZ45177.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Missouri 17; TISSUE=Seedling;
RX PubMed=30061735; DOI=10.1038/s41588-018-0182-0;
RA Sun S., Zhou Y., Chen J., Shi J., Zhao H., Zhao H., Song W., Zhang M.,
RA Cui Y., Dong X., Liu H., Ma X., Jiao Y., Wang B., Wei X., Stein J.C.,
RA Glaubitz J.C., Lu F., Yu G., Liang C., Fengler K., Li B., Rafalski A.,
RA Schnable P.S., Ware D.H., Buckler E.S., Lai J.;
RT "Extensive intraspecific gene order and gene structural variations between
RT Mo17 and other maize genomes.";
RL Nat. Genet. 50:1289-1295(2018).
CC -!- FUNCTION: Component of the volatile terpenes biosynthesis pathways
CC (Probable). Sesquiterpene synthase that converts farnesyl diphosphate
CC to (E)-beta-caryophyllene (By similarity). Involved in indirect defense
CC by producing volatile signals attracting natural enemies of herbivores
CC (By similarity). {ECO:0000250|UniProtKB:B2C4D0, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000250|UniProtKB:B2C4D0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000250|UniProtKB:B2C4D0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B2C4D0};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B2C4D0};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q5GJ60};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000250|UniProtKB:Q84ZW8}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
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:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; NCVQ01000002; PWZ45177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6G998; -.
DR SMR; A0A3L6G998; -.
DR MaizeGDB; 1204229; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Unplaced.
DR Proteomes; UP000251960; Chromosome 10.
DR ExpressionAtlas; A0A3L6G998; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; 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 3: Inferred from homology;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Plant defense;
KW Reference proteome.
FT CHAIN 1..547
FT /note="(E)-beta-caryophyllene synthase"
FT /id="PRO_0000447522"
FT MOTIF 302..306
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 547 AA; 63483 MW; 5E56D1BE164C124B CRC64;
MAADEARSVS RLHSEEDMHG KHHSTLWGDF FLHHVPCRPG QYSIMKDNVK IMKEEVKKML
LDVGSSDLSH KLECIDTLER LGLDYHYTKE IDELMCNVFE ARDQDLDLTT TSQLFYLLRK
HGYHVSSDVF LKFGDDKGDI VTDDARCLLR MYEAAHVRVN GEEILDNILI HTKRQLQCIV
DDLEPTLQEE VRYALETPLF RRLNRVQARQ FISTYEKSTT RNNMLLEFSK LDFNILLTLY
CEELKDLTMW WKEFQAQANT AIYARDRMVE MHFWMMGVFF EPQYSYSRKM LTQLFMIVSV
LDDLYDSHCT TEEGNAFTAA LQRWDEEGVE QCPTYLRTLY TNIRATVKAI EEDLNLQNNK
HAKLVKGLII DMAMCYNAET EWRDKKYVPA TVDEHLKISA RSSGCMHLVS QGFISMGDVA
TSEALEWAST YPKIVRAVCI IARLANDIMS YKREASNNTM VSTVQTCAKE YGTTTVEQAI
EKIRELIEEA WMDITHECLR QPQPMALLER AVNLARTMDF LYKDVDGYTD SRSIKGILDS
LYVDIID
