ID   TPS4A_MAIZE             Reviewed;         554 AA.
AC   Q6JD73; K7TQK8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2019, sequence version 2.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=7-epi-sesquithujene synthase {ECO:0000303|PubMed:15075399};
DE            EC=4.2.3.101 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE   AltName: Full=(E)-alpha-bergamotene synthase {ECO:0000303|PubMed:15075399};
DE            EC=4.2.3.81 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE   AltName: Full=Beta-bisabolene synthase {ECO:0000303|PubMed:15075399};
DE            EC=4.2.3.55 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE   AltName: Full=Beta-curcumene synthase {ECO:0000303|PubMed:15075399};
DE            EC=4.2.3.- {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE   AltName: Full=Beta-farnesene synthase {ECO:0000303|PubMed:15075399};
DE            EC=4.2.3.47 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE   AltName: Full=Gamma-curcumene synthase {ECO:0000303|PubMed:15075399};
DE            EC=4.2.3.94 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE   AltName: Full=Sesquisabinene A synthase {ECO:0000303|PubMed:15075399};
DE            EC=4.2.3.- {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE   AltName: Full=Terpene synthase 4 {ECO:0000303|PubMed:15075399};
DE            Short=tps4-B73 {ECO:0000303|PubMed:15075399};
GN   Name=TPS4 {ECO:0000303|PubMed:15075399};
GN   ORFNames=ZEAMMB73_Zm00001d024478 {ECO:0000312|EMBL:AQK41278.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, 3D-STRUCTURE MODELING, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. B73;
RX   PubMed=15075399; DOI=10.1105/tpc.019877;
RA   Koellner T.G., Schnee C., Gershenzon J., Degenhardt J.;
RT   "The variability of sesquiterpenes emitted from two Zea mays cultivars is
RT   controlled by allelic variation of two terpene synthase genes encoding
RT   stereoselective multiple product enzymes.";
RL   Plant Cell 16:1115-1131(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73;
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 CATALYTIC ACTIVITY.
RX   PubMed=25940560; DOI=10.1039/c5ob00711a;
RA   Vattekkatte A., Gatto N., Koellner T.G., Degenhardt J., Gershenzon J.,
RA   Boland W.;
RT   "Substrate geometry controls the cyclization cascade in multiproduct
RT   terpene synthases from Zea mays.";
RL   Org. Biomol. Chem. 13:6021-6030(2015).
RN   [4]
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: Sesquiterpene synthase involved in the production after
CC       herbivore attack of a blend of volatiles that attracts natural enemies
CC       of herbivores. Converts farnesyl diphosphate to (S)-beta-bisabolene and
CC       7-epi-sesquithujene, along with a mixture of more than 20 other minor
CC       sesquiterpene olefins. Can also act in vitro as a monoterpene synthase,
CC       converting geranyl diphosphate to (S)-(-)-limonene, beta-myrcene and 11
CC       other monoterpenes. {ECO:0000269|PubMed:15075399,
CC       ECO:0000269|PubMed:25940560}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = 7-epi-sesquithujene +
CC         diphosphate; Xref=Rhea:RHEA:31995, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:63710, ChEBI:CHEBI:175763; EC=4.2.3.101;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31996;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene +
CC         diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:62756, ChEBI:CHEBI:175763; EC=4.2.3.81;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31428;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC         diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene +
CC         diphosphate; Xref=Rhea:RHEA:28266, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:49263, ChEBI:CHEBI:175763; EC=4.2.3.55;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28267;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,6E)-farnesyl diphosphate = (-)-beta-curcumene +
CC         diphosphate; Xref=Rhea:RHEA:31419, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:62760, ChEBI:CHEBI:162247;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31420;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = gamma-curcumene + diphosphate;
CC         Xref=Rhea:RHEA:32031, ChEBI:CHEBI:33019, ChEBI:CHEBI:63696,
CC         ChEBI:CHEBI:175763; EC=4.2.3.94;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32032;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = sesquisabinene A + diphosphate;
CC         Xref=Rhea:RHEA:60020, ChEBI:CHEBI:33019, ChEBI:CHEBI:143551,
CC         ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:15075399,
CC         ECO:0000269|PubMed:25940560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60021;
CC         Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15075399};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:15075399};
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=1.1 uM for farnesyl diphosphate (in the presence of 10 mM
CC         magnesium and 1 mM manganese) {ECO:0000269|PubMed:15075399};
CC         KM=0.9 uM for geranyl diphosphate (in the presence of 10 mM magnesium
CC         and 1 mM manganese) {ECO:0000269|PubMed:15075399};
CC         KM=170 uM for magnesium (in the presence of 10 uM farnesyl
CC         diphosphate) {ECO:0000269|PubMed:15075399};
CC         KM=0.5 uM for manganese (in the presence of 10 uM farnesyl
CC         diphosphate) {ECO:0000269|PubMed:15075399};
CC         Note=Increased production of (E)-beta-farnesene the presence of
CC         manganese.;
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:15075399};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:30187155}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15075399}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the husk. Detected in leaf
CC       sheaths and leaves. {ECO:0000269|PubMed:15075399}.
CC   -!- INDUCTION: Up-regulated in leaf sheaths after herbivore damage.
CC       {ECO:0000269|PubMed:15075399}.
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: The allele found in cv. B73 encodes an active enzyme
CC       while the allele found in cv. Delprim contains a frame shift mutation
CC       (PubMed:15075399). {ECO:0000305|PubMed:15075399}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AY518310; AAS88571.1; -; mRNA.
DR   EMBL; CM000786; AQK41278.1; -; Genomic_DNA.
DR   RefSeq; NP_001292867.3; NM_001305938.3.
DR   AlphaFoldDB; Q6JD73; -.
DR   SMR; Q6JD73; -.
DR   PaxDb; 4577-Q6JD73; -.
DR   GeneID; 542754; -.
DR   KEGG; zma:542754; -.
DR   MaizeGDB; 1219892; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   HOGENOM; CLU_003125_7_2_1; -.
DR   InParanoid; Q6JD73; -.
DR   OMA; CIAPTEQ; -.
DR   OrthoDB; 1877784at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0102064; F:gamma-curcumene synthase activity; EXP:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   FunFam; 1.10.600.10:FF:000007; Isoprene synthase, chloroplastic; 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; 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; IPR050148; Terpene_synthase-like.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR31225:SF168; INACTIVE SESQUITHUJENE 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; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Plant defense;
KW   Reference proteome.
FT   CHAIN           1..554
FT                   /note="7-epi-sesquithujene synthase"
FT                   /id="PRO_0000418849"
FT   MOTIF           308..312
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         449
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         452
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   CONFLICT        4
FT                   /note="H -> P (in Ref. 1; AAS88571)"
SQ   SEQUENCE   554 AA;  63919 MW;  36265D790640E258 CRC64;
     MASHPAHRSS KAADEELPKA SSTFHPSLWG SFFLTYQPPT APQRANMKER AEVLRERVRK
     VLKGSTTDQL PETVNLILTL QRLGLGYYYE NEIDKLLHQI YSNSDYNVKD LNLVSQRFYL
     LRKNGYDVPS DVFLSFKTEE GGFACAAADT RSLLSLYNAA YLRKHGEEVL DEAISSTRLR
     LQDLLGRLLP ESPFAKEVSS SLRTPLFRRV GILEARNYIP IYETEATRNE AVLELAKLNF
     NLQQLDFCEE LKHCSAWWNE MIAKSKLTFV RDRIVEEYFW MNGACYDPPY SLSRIILTKI
     TGLITIIDDM FDTHGTTEDC MKFAEAFGRW DESAIHLLPE YMKDFYILML ETFQSFEDAL
     GPEKSYRVLY LKQAMERLVE LYSKEIKWRD DDYVPTMSEH LQVSAETIAT IALTCSAYAG
     MGDMSIRKET FEWALSFPQF IRTFGSFVRL SNDVVSTKRE QTKDHSPSTV HCYMKEHGTT
     MDDACEKIKE LIEDSWKDML EQSLALKGLP KVVPQLVFDF SRTTDNMYRD RDALTSSEAL
     KEMIQLLFVE PIPE
//