TPS2_MAIZE
ID TPS2_MAIZE Reviewed; 581 AA.
AC Q29VN2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Terpene synthase 2, chloroplastic {ECO:0000303|PubMed:27662898, ECO:0000312|EMBL:AAX99149.1};
DE AltName: Full=(3S,6E)-nerolidol synthase {ECO:0000305};
DE EC=4.2.3.48 {ECO:0000269|PubMed:27662898};
DE AltName: Full=(E,E)-geranyllinalool synthase {ECO:0000305};
DE EC=4.2.3.144 {ECO:0000269|PubMed:27662898};
DE AltName: Full=S-(+)-linalool synthase {ECO:0000305};
DE EC=4.2.3.25 {ECO:0000269|PubMed:27662898};
DE Flags: Precursor;
GN Name=TPS2 {ECO:0000303|PubMed:27662898, ECO:0000312|EMBL:AAX99149.1};
GN ORFNames=ZEAMMB73_Zm00001d015053 {ECO:0000312|EMBL:AQK67958.1};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, AND
RP PHYLOGENETIC ANALYSIS.
RC STRAIN=cv. B73;
RX PubMed=27662898; DOI=10.1105/tpc.15.00919;
RA Richter A., Schaff C., Zhang Z., Lipka A.E., Tian F., Koellner T.G.,
RA Schnee C., Preiss S., Irmisch S., Jander G., Boland W., Gershenzon J.,
RA Buckler E.S., Degenhardt J.;
RT "Characterization of biosynthetic pathways for the production of the
RT volatile homoterpenes DMNT and TMTT in Zea mays.";
RL Plant Cell 28:2651-2665(2016).
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 INDUCTION.
RX PubMed=26378100; DOI=10.1104/pp.15.01039;
RA Tzin V., Fernandez-Pozo N., Richter A., Schmelz E.A., Schoettner M.,
RA Schaefer M., Ahern K.R., Meihls L.N., Kaur H., Huffaker A., Mori N.,
RA Degenhardt J., Mueller L.A., Jander G.;
RT "Dynamic maize responses to aphid feeding are revealed by a time series of
RT transcriptomic and metabolomic assays.";
RL Plant Physiol. 169:1727-1743(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: Involved in sesquiterpene (C15), diterpene (C20) and
CC monoterpene (C10) biosynthesis. Has sesquiterpene synthase activity,
CC converting farnesyl diphosphate to nerolidol, the precursor of the
CC volatile C11-homoterpene (E)-3,8-dimethyl-1,4,7-nonatriene (DMNT). Has
CC diterpene synthase activity, converting geranylgeranyl diphosphate to
CC (E,E)-geranyllinalool, the precursor of the volatile C16-homoterpene
CC (E,E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene (TMTT). Has monoterpene
CC synthase activity, converting geranyl diphosphate into linalool. Forms
CC only the S-isomers of the three tertiary terpene alcohols.
CC {ECO:0000269|PubMed:27662898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (3S,6E)-nerolidol +
CC diphosphate; Xref=Rhea:RHEA:27530, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59958, ChEBI:CHEBI:175763;
CC EC=4.2.3.48; Evidence={ECO:0000269|PubMed:27662898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27531;
CC Evidence={ECO:0000269|PubMed:27662898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (6E,10E)-
CC geranyllinalool + diphosphate; Xref=Rhea:RHEA:38155,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:74299; EC=4.2.3.144;
CC Evidence={ECO:0000269|PubMed:27662898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38156;
CC Evidence={ECO:0000269|PubMed:27662898};
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:27662898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24117;
CC Evidence={ECO:0000269|PubMed:27662898};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O81192};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:O81192};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for farnesyl diphosphate (at pH 7.5)
CC {ECO:0000269|PubMed:27662898};
CC KM=25 uM for geranylgeranyl diphosphate (at pH 7.5)
CC {ECO:0000269|PubMed:27662898};
CC KM=16.9 uM for geranyl diphosphate (at pH 7.5)
CC {ECO:0000269|PubMed:27662898};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:27662898, ECO:0000305|PubMed:30187155}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:27662898}.
CC -!- INDUCTION: By a musk indanone elicitor that mimics herbivory. By
CC caterpillar S.littoralis oral secretions, in combination with wounding
CC (PubMed:27662898). By corn leaf aphid feeding (PubMed:26378100).
CC {ECO:0000269|PubMed:26378100, ECO:0000269|PubMed:27662898}.
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:0000255,
CC ECO:0000305}.
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DR EMBL; AY928081; AAX99149.1; -; mRNA.
DR EMBL; CM000781; AQK67958.1; -; Genomic_DNA.
DR RefSeq; NP_001105854.1; NM_001112384.1.
DR AlphaFoldDB; Q29VN2; -.
DR SMR; Q29VN2; -.
DR STRING; 4577.GRMZM2G046615_P01; -.
DR PaxDb; Q29VN2; -.
DR PRIDE; Q29VN2; -.
DR GeneID; 732758; -.
DR KEGG; zma:732758; -.
DR MaizeGDB; 9022637; -.
DR eggNOG; ENOG502QTGK; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR OMA; IAREWEV; -.
DR OrthoDB; 449049at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; Q29VN2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0080013; F:(E,E)-geranyllinalool synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0034007; F:S-linalool synthase activity; IDA:UniProtKB.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043693; P:monoterpene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0031347; P:regulation of defense response; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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; 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 Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plant defense;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..581
FT /note="Terpene synthase 2, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440867"
FT MOTIF 336..340
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81192"
SQ SEQUENCE 581 AA; 65428 MW; 791CCA20D141C837 CRC64;
MYSLPGATMS AAPASIISSS SFVEPLLLAA ASPAAAAAAA NSHHQVRQRG HLVRTLAASS
SSNTLLRSDF DLQEGLTTDV KRMLRQRQKK SGGGREMLVT IDNLKRLCID HYFEEEIEGA
MATGACTRLL HSDDLFDATL AFRLLREAGH DVSAKDDVLR RFIDGASGDF KLSLSNDVRG
LLSLHDMSHL DVGGEAALLH RAKEFSSRHL ASAVRYLDDP SLAEYVRQSL DHPYHLSLTQ
YKARHHLRYL QSLPSRDAAV ERLAVAEFQL NKSLHQGEMR EIKRWWMDLG LAEEIPVVRD
QVMKWYMWSM AALQGSSFSR YRVEITKIIS LVYVVDDIFD LVGTLEELSA FTEAVKMWDT
VAADSLPSCM RSCYKALHTV TNEIAEIAQK EHGSNHVNRL RKAWAVLFDG FMVEARWLAT
DQVPTAEDYL RNGVITSGVP LTFMHIFSML GYDDPSTEEE EEAIIDHMPS IISCPAKILR
LWDDMGSAED EAQEGFDGSY RDFYLMENPS RSPGEAEAHM RGLIAREWEV LNRECFCRRT
FPSNLVQVCL NTARMVSVMY SYNKEQRLPV LEDYAAMMLV L
