TPS4A_MAIZE
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 03-AUG-2022, entry version 82.
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 = diphosphate + gamma-curcumene;
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 = diphosphate + sesquisabinene A;
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_001292867.2; NM_001305938.2.
DR AlphaFoldDB; Q6JD73; -.
DR SMR; Q6JD73; -.
DR STRING; 4577.GRMZM2G117319_P01; -.
DR PaxDb; Q6JD73; -.
DR GeneID; 542754; -.
DR KEGG; zma:542754; -.
DR MaizeGDB; 1219892; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR OMA; NDHERIF; -.
DR OrthoDB; 360509at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; Q6JD73; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102064; F:gamma-curcumene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; 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 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
