TPS11_MAIZE
ID TPS11_MAIZE Reviewed; 548 AA.
AC Q1EG72; A0A1Q0XLC1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, 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 11 {ECO:0000303|PubMed:18524777};
GN Name=TPS11 {ECO:0000303|PubMed:18524777};
GN Synonyms=UMI3 {ECO:0000303|PubMed:15980197};
GN ORFNames=ZEAMMB73_Zm00001d024210 {ECO:0000312|EMBL:AQK40803.1};
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, MUTAGENESIS OF
RP TYR-522 AND ASP-526, INDUCTION BY HERBIVORY, AND TISSUE 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 -!- 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: Tyr-522 is involved in the initial isomerization of the
CC (E,E)-nerolidyl cation to its (Z,E)-isomer.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY647254; AAT70086.1; -; mRNA.
DR EMBL; EU716166; ACF58240.1; -; mRNA.
DR EMBL; CM000786; AQK40803.1; -; Genomic_DNA.
DR RefSeq; NP_001105950.1; NM_001112480.1.
DR RefSeq; NP_001307938.1; NM_001321009.1.
DR AlphaFoldDB; Q1EG72; -.
DR SMR; Q1EG72; -.
DR STRING; 4577.GRMZM2G127087_P03; -.
DR PaxDb; Q1EG72; -.
DR GeneID; 103641097; -.
DR KEGG; zma:103641097; -.
DR MaizeGDB; 1219887; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR OMA; THITWAR; -.
DR OrthoDB; 360509at2759; -.
DR BRENDA; 4.2.3.55; 6752.
DR BRENDA; 5.5.1.17; 6752.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; Q1EG72; baseline and differential.
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_0000412242"
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 MUTAGEN 522
FT /note="Y->F: Decreased activity and loss of production of
FT (S)-beta-macrocarpene."
FT /evidence="ECO:0000269|PubMed:18524777"
FT MUTAGEN 526
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18524777"
SQ SEQUENCE 548 AA; 63938 MW; 6CCA020476F8F42F CRC64;
MAAPTLTTDG PRLGQQEMKK MSPSFHPTLW GDFFLSYEAP TEAQEAEMRQ RAEVLREEVR
NMIKGSHDVP EIVDLIITLQ RLNLDYHYED EINEKLAVVY NSNYDGGNLD LVSRRFYLLR
KCGYHVSSDV FLNFKDQYGN FIEVDTRSLL SLYNAAYLRI HGETVLDEAI SFTTRCLQDR
LEHLESPIAE EVSSALDTPL FRRVGTLEMK DYIPIYEKDA KQNKSILEFA KLNFNLLQLL
YSSELKECTT WWKELRVESN LSFVRDRIVE VYFWMSGGCY DPQYSHSRII LTKIVAFITI
LDDTLDSHAN SYESMQLAEA VERWDESAVS LLPEYMKDFY MYLLKTFSSF ENELGPDKSY
RVFYLKEAVK ELVREYTKEI KWRDEDYVPK TLKEHLKVSL ISIGGTLVLC SAFVGMGDVV
TKKIMEWVMS DAELVKSFGI FVRLSNDIVS TKREQREKHC VSTVQCYMKQ HELTMDEACE
QIKELTEDSW KFMIEQGLAL KEYPIIVPRT VLEFARTVDY MYKEADKYTV SHTIKDMLTS
LYVKPVLM