TS23B_MAIZE
ID TS23B_MAIZE Reviewed; 547 AA.
AC B2C4D0; A0A1D6IYC6; B2C4D2;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=(E)-beta-caryophyllene synthase {ECO:0000303|PubMed:18296628};
DE EC=4.2.3.57 {ECO:0000269|PubMed:18296628};
DE AltName: Full=Terpene synthase 23 {ECO:0000303|PubMed:30187155};
GN Name=TPS23 {ECO:0000303|PubMed:30187155};
GN ORFNames=ZEAMMB73_Zm00001d024234 {ECO:0000312|EMBL:AQK40889.1};
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP INDUCTION BY HERBIVORES, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. B73, and cv. Delprim;
RX PubMed=18296628; DOI=10.1105/tpc.107.051672;
RA Koellner T.G.J., Held M., Lenk C., Hiltpold I., Turlings T.C.,
RA Gershenzon J., Degenhardt J.;
RT "A maize (E)-beta-caryophyllene synthase implicated in indirect defense
RT responses against herbivores is not expressed in most American maize
RT varieties.";
RL Plant Cell 20:482-494(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP FUNCTION, AND INDUCTION BY HERBIVORES.
RC STRAIN=cv. B73 Inbred, cv. Braz1006, and cv. Delprim;
RX PubMed=28428873; DOI=10.1002/ece3.2893;
RA Tamiru A., Bruce T.J.A., Richter A., Woodcock C.M., Midega C.A.O.,
RA Degenhardt J., Kelemu S., Pickett J.A., Khan Z.R.;
RT "A maize landrace that emits defense volatiles in response to herbivore
RT eggs possesses a strongly inducible terpene synthase gene.";
RL Ecol. Evol. 7:2835-2845(2017).
RN [4]
RP FUNCTION, AND INDUCTION BY HERBIVORES.
RC STRAIN=cv. Mp708, and cv. Texas 601;
RX PubMed=29151152; DOI=10.1007/s10886-017-0904-2;
RA Castano-Duque L., Loades K.W., Tooker J.F., Brown K.M., Paul Williams W.,
RA Luthe D.S.;
RT "A maize inbred exhibits resistance against western corn rootwoorm,
RT Diabrotica virgifera virgifera.";
RL J. Chem. Ecol. 43:1109-1123(2017).
RN [5]
RP REVIEW.
RX PubMed=30187155; DOI=10.1007/s00425-018-2999-2;
RA Block A.K., Vaughan M.M., Schmelz E.A., Christensen S.A.;
RT "Biosynthesis and function of terpenoid defense compounds in maize (Zea
RT mays).";
RL Planta 249:21-30(2019).
CC -!- FUNCTION: Component of the volatile terpenes biosynthesis pathways
CC (PubMed:30187155). Sesquiterpene synthase that converts farnesyl
CC diphosphate to (E)-beta-caryophyllene (PubMed:18296628). Involved in
CC indirect defense by producing volatile signals that attract natural
CC enemies of leaf herbivores such as Chilo partellus and root herbivores
CC like the western corn rootworm (WCR, Diabrotica virgifera) and fall
CC armyworm (Spodoptera littoralis and Spodoptera frugiperda)
CC (PubMed:18296628, PubMed:28428873, PubMed:29151152). Deters leaf
CC herbivores by triggering (E)-beta-caryophyllene production upon insect
CC (stemborer C.partellus) egg deposition; (E)-beta-caryophyllene attracts
CC the parasitic wasp Cotesia sesamiae which lays eggs on the larvae of
CC C.partellus, which is ultimately fatal (PubMed:28428873).
CC {ECO:0000269|PubMed:18296628, ECO:0000269|PubMed:28428873,
CC ECO:0000269|PubMed:29151152, ECO:0000303|PubMed:30187155}.
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:0000269|PubMed:18296628};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:18296628};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18296628};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18296628};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q5GJ60};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for farnesyl diphosphate (in the presence of MgCl(2))
CC {ECO:0000269|PubMed:18296628};
CC KM=1.1 uM for farnesyl diphosphate (in the presence of MnCl(2))
CC {ECO:0000269|PubMed:18296628};
CC Note=kcat is 0.00191 sec(-1) with farnesyl diphosphate (in the
CC presence of MgCl(2)). kcat is 0.0013 sec(-1) with farnesyl
CC diphosphate (in the presence of MnCl(2)).
CC {ECO:0000269|PubMed:18296628};
CC pH dependence:
CC Optimum pH is 8-9.5. {ECO:0000269|PubMed:18296628};
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 -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:18296628}.
CC -!- INDUCTION: Induced by Diabrotica virgifera damage in roots and
CC Spodoptera littoralis damage in leaves (PubMed:18296628,
CC PubMed:29151152). Accumulates upon stemborer Chilo partellus eggs
CC deposition in some cultivars (e.g. cv. Braz1006) but less in others
CC (e.g. cv. Delprim and cv. B73) (PubMed:28428873).
CC {ECO:0000269|PubMed:18296628, ECO:0000269|PubMed:28428873,
CC ECO:0000269|PubMed:29151152}.
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 -!- MISCELLANEOUS: More abundant in insect resistant cultivars (e.g. cv.
CC Mp708) than in insect sensitive cultivars (e.g. cv. Tx601).
CC {ECO:0000269|PubMed:29151152}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AQK40889.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The scent of guile - Issue
CC 216 of August 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/216/";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Lure - Issue 218 of October
CC 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/218/";
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DR EMBL; EU259633; ABY79206.1; -; mRNA.
DR EMBL; EU259634; ABY79207.1; -; Genomic_DNA.
DR EMBL; EU259635; ABY79208.1; -; mRNA.
DR EMBL; CM000786; AQK40889.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_008662702.1; XM_008664480.1.
DR AlphaFoldDB; B2C4D0; -.
DR SMR; B2C4D0; -.
DR STRING; 4577.GRMZM2G127336_P01; -.
DR EnsemblPlants; Zm00001eb413120_T001; Zm00001eb413120_P001; Zm00001eb413120.
DR GeneID; 103641105; -.
DR Gramene; Zm00001eb413120_T001; Zm00001eb413120_P001; Zm00001eb413120.
DR KEGG; zma:103641105; -.
DR MaizeGDB; 1204229; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:MON-14917; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; B2C4D0; 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:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:1901937; P:beta-caryophyllene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0002213; P:defense response to insect; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0045339; P:farnesyl diphosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid 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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Plant defense;
KW Reference proteome.
FT CHAIN 1..547
FT /note="(E)-beta-caryophyllene synthase"
FT /id="PRO_0000447521"
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"
FT CONFLICT 143
FT /note="N -> K (in Ref. 1; ABY79208)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="F -> C (in Ref. 1; ABY79208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 63658 MW; 061CA21C884252F4 CRC64;
MAADEARSVS RLHSEEDMHG KHHSTLWGDF FLHHVPCRPG QYLIMKDNVE IMKEEVKKML
LDVGSSDLSH KLDCIDTLER LGLDYHYTKE IDELMCNVFE ARDQDLDLTT TSQLFYLLRK
HGYHISSDVF LKFRDDKGDI VTNDARCLLR MYEAAHVRVN GEEILDNILI HTKRQLQCIV
DDLEPTLQEE VRYALETPLF RRLNRVQARQ FISTYEKSTT RINMLLEFSK LDFNILLTLY
CEELKDLTLW WKEFQAQANT TIYARDRMVE MHFWMMGVFF EPQYSYSRKM LTQLFMIVSV
LDDLYDSHCT TEEGNAFTAA LQRWDEEGVE QCPTYLRTLY TNIRATIKAI EEDLNFQNNK
HAKLVKGLII DMAMCYNAET EWRDKKYVPA TVDEHLKISA RSSGCMHLVS QGFISMGDVA
TSEALEWAST YPKIVRAVCI IARLANDIMS YKREASNNTM VSTVQTCAKE YGTTTVEQAI
EKIRELIEEA WMDITHECLR QPQPKALLER AVNLARTMDF LYKDADGYTD SRSIKGILDS
LYVHLID
