TPS6_MAIZE
ID TPS6_MAIZE Reviewed; 548 AA.
AC Q5GJ60; A0A1Q0XLD3; Q4L0R7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=(S)-beta-macrocarpene synthase {ECO:0000303|PubMed:18524777};
DE EC=5.5.1.17 {ECO:0000269|PubMed:18524777};
DE AltName: Full=Alpha-terpinolene synthase {ECO:0000303|PubMed:18524777};
DE EC=4.2.3.113 {ECO:0000269|PubMed:18524777};
DE AltName: Full=Beta-bisabolene synthase {ECO:0000303|PubMed:18524777};
DE EC=4.2.3.55 {ECO:0000269|PubMed:18524777};
DE AltName: Full=Beta-myrcene synthase {ECO:0000303|PubMed:18524777};
DE EC=4.2.3.15 {ECO:0000269|PubMed:18524777};
DE AltName: Full=Limonene synthase {ECO:0000303|PubMed:18524777};
DE EC=4.2.3.16 {ECO:0000269|PubMed:18524777};
DE AltName: Full=Linalool synthase {ECO:0000303|PubMed:18524777};
DE EC=4.2.3.25 {ECO:0000269|PubMed:18524777};
DE AltName: Full=Terpene synthase 6 {ECO:0000303|PubMed:18524777};
GN Name=TPS6 {ECO:0000303|PubMed:18524777};
GN Synonyms=UMI2 {ECO:0000303|PubMed:15980197};
GN ORFNames=ZEAMMB73_Zm00001d024207 {ECO:0000312|EMBL:AQK40792.1};
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], AND INDUCTION BY FUNGI.
RC STRAIN=cv. Golden Bantam early;
RX PubMed=15980197; DOI=10.1104/pp.105.061200;
RA Basse C.W.;
RT "Dissecting defense-related and developmental transcriptional responses of
RT maize during Ustilago maydis infection and subsequent tumor formation.";
RL Plant Physiol. 138:1774-1784(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY HERBIVORY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. B73;
RX PubMed=18524777; DOI=10.1074/jbc.m802682200;
RA Koellner T.G., Schnee C., Li S., Svatos A., Schneider B., Gershenzon J.,
RA Degenhardt J.;
RT "Protonation of a neutral (S)-beta-bisabolene intermediate is involved in
RT (S)-beta-macrocarpene formation by the maize sesquiterpene synthases TPS6
RT and TPS11.";
RL J. Biol. Chem. 283:20779-20788(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP INDUCTION BY FUNGUS.
RX PubMed=28931629; DOI=10.1104/pp.17.00879;
RA Ding Y., Huffaker A., Koellner T.G., Weckwerth P., Robert C.A.M.,
RA Spencer J.L., Lipka A.E., Schmelz E.A.;
RT "Selinene volatiles are essential precursors for maize defense promoting
RT fungal pathogen resistance.";
RL Plant Physiol. 175:1455-1468(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: Involved in the biosynthesis of the bicyclic sesquiterpene
CC (S)-beta-macrocarpene. Can use both geranyl diphosphate and farnesyl
CC diphosphate as substrate, but not geranylgeranyl diphosphate. Produces
CC mainly (S)-beta-macrocarpene, but also smaller amounts of beta-
CC bisabolene and (E)-beta-farnesene when used with farnesyl diphosphate
CC as substrate. In the presence of geranyl diphosphate, produces the
CC acyclic monoterpenes beta-myrcene and linalool along with minor amounts
CC of the cyclic compounds limonene, alpha-thujene, sabinene and alpha-
CC terpinolene. May be involved in plant defense.
CC {ECO:0000269|PubMed:18524777}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-beta-bisabolene = (S)-beta-macrocarpene;
CC Xref=Rhea:RHEA:28282, ChEBI:CHEBI:49263, ChEBI:CHEBI:61344;
CC EC=5.5.1.17; Evidence={ECO:0000269|PubMed:18524777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28283;
CC Evidence={ECO:0000269|PubMed:18524777};
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:18524777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28267;
CC Evidence={ECO:0000269|PubMed:18524777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate;
CC Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.16;
CC Evidence={ECO:0000269|PubMed:18524777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12870;
CC Evidence={ECO:0000269|PubMed:18524777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:18524777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:18524777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
CC Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.113;
CC Evidence={ECO:0000269|PubMed:18524777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
CC Evidence={ECO:0000269|PubMed:18524777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-linalool + diphosphate;
CC Xref=Rhea:RHEA:24116, ChEBI:CHEBI:98, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.25;
CC Evidence={ECO:0000269|PubMed:18524777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24117;
CC Evidence={ECO:0000269|PubMed:18524777};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:18524777};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:18524777};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000305|PubMed:18524777};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for farnesyl diphosphate {ECO:0000269|PubMed:18524777};
CC KM=1.1 uM for geranyl diphosphate {ECO:0000269|PubMed:18524777};
CC KM=130.7 uM for magnesium (in the presence of 10 uM farnesyl
CC diphosphate) {ECO:0000269|PubMed:18524777};
CC KM=23.4 uM for manganese (in the presence of 10 uM farnesyl
CC diphosphate) {ECO:0000269|PubMed:18524777};
CC pH dependence:
CC Optimum pH is 7.0. Higher pH values favor the formation of (S)-beta-
CC bisabolene. {ECO:0000269|PubMed:18524777};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:30187155}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. Not detected in leaves, unless
CC damaged by herbivory or infected by fungi.
CC {ECO:0000269|PubMed:18524777}.
CC -!- INDUCTION: Up-regulated by herbivory and fungi (e.g. Fusarium spp.,
CC C.heterostrophus, F.verticillioides, R.microsporus and A.parasiticus).
CC {ECO:0000269|PubMed:15980197, ECO:0000269|PubMed:18524777,
CC ECO:0000269|PubMed:28931629}.
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: In the presence of magnesium, the product spectrum is
CC shifted toward an increased production of (S)-beta-bisabolene and a
CC decreased production of (S)-beta-macrocarpene.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AY647253; AAT70085.1; -; mRNA.
DR EMBL; AY518315; AAS88576.1; -; mRNA.
DR EMBL; CM000786; AQK40792.1; -; Genomic_DNA.
DR EMBL; CM000786; AQK40795.1; -; Genomic_DNA.
DR RefSeq; NP_001105674.1; NM_001112204.1.
DR AlphaFoldDB; Q5GJ60; -.
DR SMR; Q5GJ60; -.
DR PRIDE; Q5GJ60; -.
DR GeneID; 542688; -.
DR KEGG; zma:542688; -.
DR MaizeGDB; 1219887; -.
DR HOGENOM; CLU_003125_7_2_1; -.
DR OMA; TGHEFEQ; -.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:MON-15969; -.
DR BRENDA; 4.2.3.55; 6752.
DR BRENDA; 5.5.1.17; 6752.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; Q5GJ60; baseline and differential.
DR Genevisible; Q5GJ60; ZM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0034007; F:S-linalool synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEP:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; Isomerase; Lyase; Magnesium; Manganese; Metal-binding;
KW Plant defense; Reference proteome.
FT CHAIN 1..548
FT /note="(S)-beta-macrocarpene synthase"
FT /id="PRO_0000412241"
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 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
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 198
FT /note="T -> A (in Ref. 1; AAT70085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 63731 MW; BC55B95C9F131275 CRC64;
MAAPTLTADG PRLGQQEMKK MSPSFHPTLW GDFFLSYEAP TEAQEAQMRE KAAVLKEEVR
NMIKGSHDVP EIVDLIITLQ RLNLDYHYED EINEKLTVVY KSNYDGGNLD LVSRRFYLLR
KCGYDVSSDV FLKFKDQLGN FVEADTRSLL SLYNAAFLRI HGETVLDEAI SFTMRVLQDR
LEHLESPLAE EVSSALDTPL FRRVGTLEMK DYIPIYEKDA KQNKSILEFA KLNFNLLQLR
YSSELKECTT WWKELRVESN LSFVRDRIVE VYFWMSGGCY DPQYSHSRII LTKIVAFITI
LDDTLDSHAT SCESMQLAEA IERWDESAVS LLPEYMKDFY MYLLKTFSSF ENELGPDKSY
RVFYLKEAVK ELVREYTKEI KWRDEDYVPK TLKEHLKVSL ISIGGTLVLC SAFVGMGDVV
TKKIMKWVMS DAELVKSFGI FVRLSNDIVS TKREQREKHC VSTVQCYMKQ HEITMDEACE
QIKELTEDSW KFMIEQGLAL KEYPIIVPRT VLEFARTVDY MYKEADKYTV SHTIKDMLTS
LYVKPVLM
