TPS26_MAIZE
ID TPS26_MAIZE Reviewed; 627 AA.
AC A0A1D6LTV0; A5YZT5; B4F964; C0PNL6;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Alpha-terpineol synthase, chloroplastic {ECO:0000303|PubMed:18218975};
DE EC=4.2.3.111 {ECO:0000269|PubMed:18218975};
DE AltName: Full=4-terpineol synthase {ECO:0000303|PubMed:18218975};
DE EC=4.2.3.- {ECO:0000269|PubMed:18218975};
DE AltName: Full=Alpha-terpinolene synthase {ECO:0000303|PubMed:18218975};
DE EC=4.2.3.113 {ECO:0000269|PubMed:18218975};
DE AltName: Full=Beta-myrcene synthase {ECO:0000303|PubMed:18218975};
DE EC=4.2.3.15 {ECO:0000269|PubMed:18218975};
DE AltName: Full=Gamma-terpinene synthase {ECO:0000303|PubMed:18218975};
DE EC=4.2.3.114 {ECO:0000269|PubMed:18218975};
DE AltName: Full=Limonene synthase {ECO:0000303|PubMed:18218975};
DE EC=4.2.3.16 {ECO:0000269|PubMed:18218975};
DE AltName: Full=Terpene synthase 26, chloroplastic {ECO:0000303|PubMed:30187155};
DE Flags: Precursor;
GN Name=TPS26 {ECO:0000303|PubMed:30187155};
GN ORFNames=ZEAMMB73_Zm00001d037092 {ECO:0000312|EMBL:AQK82824.1};
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] (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, INDUCTION BY WOUNDING, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. KI3, and cv. McC;
RX PubMed=18218975; DOI=10.1104/pp.107.109553;
RA Lin C., Shen B., Xu Z., Koellner T.G., Degenhardt J., Dooner H.K.;
RT "Characterization of the monoterpene synthase gene tps26, the ortholog of a
RT gene induced by insect herbivory in maize.";
RL Plant Physiol. 146:940-951(2008).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 2-627 (ISOFORMS 1 AND 2).
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
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: Component of the volatile terpenes biosynthesis pathways
CC (PubMed:30187155). Mediates the synthesis of a blend of monoterpenes.
CC Converts mainly geranyl diphosphate to alpha-terpineol. Triggers also
CC the biosynthesis of minor monoterpenes including limonene, gamma-
CC terpinene, beta-myrcene, terpinolene and 4-terpineol (PubMed:18218975).
CC {ECO:0000269|PubMed:18218975, ECO:0000303|PubMed:30187155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol +
CC diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC EC=4.2.3.111; Evidence={ECO:0000269|PubMed:18218975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552;
CC Evidence={ECO:0000269|PubMed:18218975};
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:18218975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12870;
CC Evidence={ECO:0000269|PubMed:18218975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene;
CC Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.114;
CC Evidence={ECO:0000269|PubMed:18218975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560;
CC Evidence={ECO:0000269|PubMed:18218975};
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:18218975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:18218975};
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:18218975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
CC Evidence={ECO:0000269|PubMed:18218975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = 4-terpineol + diphosphate;
CC Xref=Rhea:RHEA:60028, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057, ChEBI:CHEBI:78884;
CC Evidence={ECO:0000269|PubMed:18218975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60029;
CC Evidence={ECO:0000269|PubMed:18218975};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B2C4D0};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B2C4D0};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q5GJ60};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:30187155}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18218975}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A1D6LTV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1D6LTV0-2; Sequence=VSP_060200, VSP_060201;
CC -!- TISSUE SPECIFICITY: Expressed in seedling leaf sheaths and roots.
CC {ECO:0000269|PubMed:18218975}.
CC -!- INDUCTION: Induced by wounding in roots and leaves sheaths.
CC {ECO:0000269|PubMed:18218975}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACF78657.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EF599329; ABR09288.1; -; Genomic_DNA.
DR EMBL; EF599330; ABR09289.1; -; mRNA.
DR EMBL; CM000782; AQK82824.1; -; Genomic_DNA.
DR EMBL; BT033652; ACF78657.1; ALT_INIT; mRNA.
DR EMBL; BT069885; ACN36782.1; -; mRNA.
DR RefSeq; NP_001106050.2; NM_001112580.2.
DR AlphaFoldDB; A0A1D6LTV0; -.
DR SMR; A0A1D6LTV0; -.
DR STRING; 4577.GRMZM2G030583_P03; -.
DR GeneID; 100125649; -.
DR KEGG; zma:100125649; -.
DR MaizeGDB; 651520; -.
DR OMA; ELHINIM; -.
DR OrthoDB; 360509at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; A0A1D6LTV0; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102903; F:gamma-terpinene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009611; P:response to wounding; IEP: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 Alternative splicing; Chloroplast; Cobalt; Lyase; Magnesium; Manganese;
KW Metal-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..627
FT /note="Alpha-terpineol synthase, chloroplastic"
FT /id="PRO_0000447523"
FT REGION 13..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 376..380
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 73..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT VAR_SEQ 1..323
FT /note="MAGITGVMNMKLAARPSSGRHSRGCRPAVVPSAGKQMLLVRRHPPGSASWPT
FT RATGGGGGGVPAGATAADSSGQAKEEEEEDRASRNTSSFEPSIWGDFFLTYSSPLATSS
FT AQKARMVHRAEQLKKQVAKLIAASGACSLYHRIHLVDALERLCLDYLFEDEINDMVTQI
FT HNVDVSGCDLQTVAMWFYLLRNHGYRVSSDVVFAKFRDEQGGFAANNPRDLLNLYNAAC
FT LRTHGETILDEAASFTSKCLKSLAPYTYMEASLASEIKRALEIPLPRSVRIYGAKSRIA
FT EYGNQTEANELVLELAKLNYNLVQLQHQEELKIIT -> MS (in isoform 2)"
FT /id="VSP_060200"
FT VAR_SEQ 547..627
FT /note="Missing (in isoform 2)"
FT /id="VSP_060201"
FT CONFLICT 126
FT /note="K -> E (in Ref. 1; ABR09288/ABR09289)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="N -> K (in Ref. 1; ABR09288/ABR09289)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="Q -> R (in Ref. 1; ABR09288/ABR09289)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="Y -> D (in Ref. 3; ACF78657)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="S -> N (in Ref. 1; ABR09288/ABR09289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 70785 MW; 8DDE369A8980506F CRC64;
MAGITGVMNM KLAARPSSGR HSRGCRPAVV PSAGKQMLLV RRHPPGSASW PTRATGGGGG
GVPAGATAAD SSGQAKEEEE EDRASRNTSS FEPSIWGDFF LTYSSPLATS SAQKARMVHR
AEQLKKQVAK LIAASGACSL YHRIHLVDAL ERLCLDYLFE DEINDMVTQI HNVDVSGCDL
QTVAMWFYLL RNHGYRVSSD VVFAKFRDEQ GGFAANNPRD LLNLYNAACL RTHGETILDE
AASFTSKCLK SLAPYTYMEA SLASEIKRAL EIPLPRSVRI YGAKSRIAEY GNQTEANELV
LELAKLNYNL VQLQHQEELK IITRWWNDLE LQTRLSFARD RVVECYFWMV GVYFEPSYSR
ARVILSKVLA IVSLLDDTYD VYGTSQECEL FTKCIESWDP AATGGRLPGN MKFIFAKILD
TCQSFEDELA PDEKYRMHYL KTFIIDLVRA YNEEVKWREQ GYVPATVEEH LQVSARSGGC
HLLSCTSFVG MGDVADQEAF EWVRGVPKIV KALCIILRLS DDLKSYEREK MSSHVASTME
SCMKEHQVPL EVARVKIQET IDETWKDFNE EWLNLNTNSH LPRELLERIF NLTRTMVYIY
QQDDAYTNCH VIKDTINSLF VEPVSIT
