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TPS5C_MAIZE
ID   TPS5C_MAIZE             Reviewed;         554 AA.
AC   Q6JD72; K7TQL5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2019, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Inactive sesquithujene synthase {ECO:0000303|PubMed:15075399};
DE   AltName: Full=Terpene synthase 5 {ECO:0000303|PubMed:15075399};
DE            Short=tps5-B73 {ECO:0000303|PubMed:15075399};
GN   Name=TPS5 {ECO:0000303|PubMed:15075399};
GN   ORFNames=ZEAMMB73_Zm00001d024481 {ECO:0000312|EMBL:AQK41282.1};
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 MUTAGENESIS OF TRP-163; THR-383; GLU-391;
RP   LYS-402; GLU-455 AND ILE-479.
RC   STRAIN=cv. B73;
RX   PubMed=15075399; DOI=10.1105/tpc.019877;
RA   Koellner T.G., Schnee C., Gershenzon J., Degenhardt J.;
RT   "The variability of sesquiterpenes emitted from two Zea mays cultivars is
RT   controlled by allelic variation of two terpene synthase genes encoding
RT   stereoselective multiple product enzymes.";
RL   Plant Cell 16:1115-1131(2004).
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   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: Non-functional sesquiterpene synthase having less than 1% of
CC       the activity found in cv. Delprim.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q6JD73};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q6JD73};
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: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
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: The allele found in cv. B73 encodes an inactive enzyme
CC       while the two alleles found in cv. Delprim encode an active (TPS5A) and
CC       an inactive (TPS5B) enzyme (PubMed:15075399).
CC       {ECO:0000305|PubMed:15075399}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AY518311; AAS88572.1; -; mRNA.
DR   EMBL; CM000786; AQK41282.1; -; Genomic_DNA.
DR   RefSeq; NP_001288477.1; NM_001301548.1.
DR   AlphaFoldDB; Q6JD72; -.
DR   SMR; Q6JD72; -.
DR   STRING; 4577.GRMZM2G074309_P01; -.
DR   PaxDb; Q6JD72; -.
DR   EnsemblPlants; Zm00001eb415130_T001; Zm00001eb415130_P001; Zm00001eb415130.
DR   GeneID; 103641226; -.
DR   Gramene; Zm00001eb415130_T001; Zm00001eb415130_P001; Zm00001eb415130.
DR   KEGG; zma:103641226; -.
DR   MaizeGDB; 1219892; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   HOGENOM; CLU_003125_7_2_1; -.
DR   OMA; KECIKTT; -.
DR   OrthoDB; 360509at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000007305; Chromosome 10.
DR   ExpressionAtlas; Q6JD72; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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; Magnesium; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..554
FT                   /note="Inactive sesquithujene synthase"
FT                   /id="PRO_0000418853"
FT   MOTIF           308..312
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         449
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         452
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   MUTAGEN         163
FT                   /note="W->R: Restore 60% of the activity found in cv.
FT                   Delprim, ableit with an increased production of (E)-beta-
FT                   farnesene. Full activity; when associated with V-455."
FT                   /evidence="ECO:0000269|PubMed:15075399"
FT   MUTAGEN         383
FT                   /note="T->S: No effect on the absence of activity."
FT                   /evidence="ECO:0000269|PubMed:15075399"
FT   MUTAGEN         391
FT                   /note="E->Q: No effect on the absence of activity."
FT                   /evidence="ECO:0000269|PubMed:15075399"
FT   MUTAGEN         402
FT                   /note="K->Q: No effect on the absence of activity."
FT                   /evidence="ECO:0000269|PubMed:15075399"
FT   MUTAGEN         455
FT                   /note="E->V: Restore 4% of the activity found in cv.
FT                   Delprim, but with the same blend of products. Full
FT                   activity; when associated with R-163."
FT                   /evidence="ECO:0000269|PubMed:15075399"
FT   MUTAGEN         479
FT                   /note="I->T: No effect on the absence of activity."
FT                   /evidence="ECO:0000269|PubMed:15075399"
FT   CONFLICT        20
FT                   /note="A -> V (in Ref. 1; AAS88572)"
SQ   SEQUENCE   554 AA;  63841 MW;  632454E27D3D387C CRC64;
     MASPPAHRSS KAADEELPKA SSTFHPSLWG SFFLTYQPPT APQRANMKER AEVLRERVRK
     VLKGSTTDQL PETVNLILTL QRLGLGYYYE NEIDKLLHQI YSNSDYNVKD LNLVSQRFYL
     LRKNGYDVPS DVFLSFKTEE GGFACAAADT RSLLSLYNAA YLWKHGEEVL DEAISSTRLR
     LQDLLGRLLP ESPFAKEVSS SLRTPLFRRV GILEARNYIP IYETEATRNE AVLELAKLNF
     NLQQLDFCEE LKHCSAWWNE MIAKSKLTFV RDRIVEEYFW MNGACYDPPY SLSRIILTKI
     TGLITIIDDM FDTHGTTEDC MKFAEAFGRW DESAIHLLPE YMKDFYILML ETFQSFEDAL
     GPEKSYRVLY LKQAMERLVE LYTKEIKWRD EDYVATMSEH LKVSAESIGA NALTCSAYAG
     MGDMSITKET FEWALSFPQF IRTFGSFVRL SNDVESTKRE QTKDHSPSTV HCYMKEHGIT
     MDDACEKIKE LIEDSWKDML EQSLALKGLP KVVPQLVFDF SRTTDNMYRD RDALTSSEAL
     KEMIQLLFVE PIPE
 
 
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