TPS7_MAIZE
ID TPS7_MAIZE Reviewed; 548 AA.
AC Q5GJ59; A0A1D6KPD6; B6SPA6;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Tau-cadinol synthase {ECO:0000303|PubMed:27421723};
DE EC=4.2.3.173 {ECO:0000269|PubMed:27421723};
DE AltName: Full=Terpene synthase 7 {ECO:0000303|Ref.1};
DE Short=ZmTPS7 {ECO:0000303|PubMed:27421723};
GN Name=TPS7 {ECO:0000303|Ref.1};
GN ORFNames=ZEAMMB73_Zm00001d032230 {ECO:0000312|EMBL:ONM04668.1};
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].
RC STRAIN=cv. B73;
RA Koellner T.G., Schnee C., Gershenzon J., Degenhardt J.;
RT "Evolution and functional diversity of the terpene synthase family in
RT maize.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY ABSCISIC
RP ACID; FUNGUS SPORE AND METHYL JASMONATE, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP COFACTOR.
RC STRAIN=cv. Missouri 17;
RX PubMed=27421723; DOI=10.1007/s00425-016-2570-y;
RA Ren F., Mao H., Liang J., Liu J., Shu K., Wang Q.;
RT "Functional characterization of ZmTPS7 reveals a maize tau-cadinol synthase
RT involved in stress response.";
RL Planta 244:1065-1074(2016).
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: Sesquiterpene synthase that catalyzes the formation of a
CC blend of sesquiterpenes and sesquiterpenoid alcohols (PubMed:27421723).
CC Converts farnesyl diphosphate to tau-cadinol (PubMed:27421723).
CC {ECO:0000269|PubMed:27421723}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + tau-
CC cadinol; Xref=Rhea:RHEA:54052, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138042, ChEBI:CHEBI:175763; EC=4.2.3.173;
CC Evidence={ECO:0000269|PubMed:27421723};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54053;
CC Evidence={ECO:0000269|PubMed:27421723};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:27421723};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q6JD73};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:27421723};
CC Note=kcat is 0.00136 sec(-1) with (2E,6E)-farnesyl diphosphate as
CC substrate. {ECO:0000269|PubMed:27421723};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:27421723};
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: Constitutively expressed in aerial tissues, but
CC barely observed in roots. {ECO:0000269|PubMed:27421723}.
CC -!- INDUCTION: Induced by fungus spore (F. graminearum) inoculation and
CC methyl jasmonate (MeJA) treatment in leaves (PubMed:27421723).
CC Triggered by abscisic acid (ABA) in roots (PubMed:27421723).
CC {ECO:0000269|PubMed:27421723}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ONM04668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY518316; AAS88577.1; -; mRNA.
DR EMBL; CM007647; ONM04668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EU954571; ACG26689.1; -; mRNA.
DR RefSeq; NP_001105249.1; NM_001111779.1.
DR AlphaFoldDB; Q5GJ59; -.
DR SMR; Q5GJ59; -.
DR STRING; 4577.AC217050.4_FGP007; -.
DR PaxDb; Q5GJ59; -.
DR EnsemblPlants; Zm00001eb041770_T001; Zm00001eb041770_P001; Zm00001eb041770.
DR GeneID; 542156; -.
DR Gramene; Zm00001eb041770_T001; Zm00001eb041770_P001; Zm00001eb041770.
DR KEGG; zma:542156; -.
DR MaizeGDB; 9035353; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_0_1; -.
DR OrthoDB; 360509at2759; -.
DR BRENDA; 4.2.3.173; 6752.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q5GJ59; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; 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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..548
FT /note="Tau-cadinol synthase"
FT /id="PRO_0000447515"
FT MOTIF 303..307
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT CONFLICT 214
FT /note="Y -> YS (in Ref. 3; ACG26689)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="H -> R (in Ref. 3; ACG26689)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="E -> Q (in Ref. 3; ACG26689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 62575 MW; A9903D0F30D4CC0E CRC64;
MATTGTTSMP APVFHPTVWG DYFIKFVPEP LQVSDETMAE RIRHLREEVS GMFQACKNVV
DKTNLVDVVQ RLGIDHHFEE QIATALASIH SAGLFNSSSL HEAALRFRLL RQQGFWVPAD
ELVKFIKNED GSFIDGITND PKGLLSLYNA AHLVTHDEGT TTLEDAIAFA RQHLEAARRC
SLKSPLAEQV GRALGIPLPR TLKREEAIAF IPEYSSQQDQ QVYSPVILEL AKLDFNLLQH
LHQEELKEIS QWWKDLSGEI GLGYVRDRIV ECYFWSYTVH YERGQARARM ILAKVFMLTS
LLDDTYDVHA TLEEARELNK AIQRWDESDV SLLPEYLKKF FVKVISNFRE FEDELESHEK
YRNVYNIKGF QTLSKHYLQE AEWFHHGCTP SFKDQVNVSV ITGGAQVLSI GLLVGMGHEA
TREAFEWAIG DTDAIWACGE VSRFMDDMSA FKNGRNKMDV ASSVECYIKE HNVPSEVALA
RINSLVEDAW KTINQAPFKY PALFPVVQRV TSLAKSMTLL FLDKRDAYTY SKDFQTTLET
HFVRHIPL
