TPS4B_MAIZE
ID TPS4B_MAIZE Reviewed; 460 AA.
AC Q6JD71;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Inactive 7-epi-sesquithujene synthase {ECO:0000303|PubMed:15075399};
DE AltName: Full=Terpene synthase 4 {ECO:0000303|PubMed:15075399};
DE Short=tps4-Del1 {ECO:0000303|PubMed:15075399};
GN Name=TPS4 {ECO:0000303|PubMed:15075399};
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. Delprim;
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 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 due to a frameshift
CC removing part of the catalytic site.
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 active enzyme
CC while the allele found in cv. Delprim contains a frame shift mutation
CC (PubMed:15075399). {ECO:0000305|PubMed:15075399}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AY518312; AAS88573.1; -; mRNA.
DR AlphaFoldDB; Q6JD71; -.
DR SMR; Q6JD71; -.
DR MaizeGDB; 1219892; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q6JD71; 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 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; 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 SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..460
FT /note="Inactive 7-epi-sesquithujene synthase"
FT /id="PRO_0000418850"
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"
SQ SEQUENCE 460 AA; 53208 MW; 6305EFCFDE4ADFBA CRC64;
MASPPAHRSS KAADEELPKA SSTFHPSLWG SFFLTYQPPT APQRANMEER AEVLRERVRK
VLKGSTTDQL PETVNLILTL QRLGLGYYYE NEIDKLLHQI YSNSDYNEKD LNLVSQRFYL
LRKNGYDVPS DVFLSFKTEE GGFACAAADT RSLLSLYNAA HLRKHGEEVL DEAISSTRLR
LQDLLGRLLP ESPFAKEVSS SLRTPLFRRV GILEARNYIP IYEKEATRNE AVLELAKLNF
NLQQLDFCEE LKHCSAWWNE MIAKSKLTFV RDRIVEEYFW MNGACYDPPY SLSRIILTKI
TGLITIIDDM FDTHGTTEDC MKFAEAFGRW DESAIHLLPE YMKDFYILML ETFQSFEDAL
GPEKSYRVLY LKQAMERLVE LYSKEIKWRD DDYVPTMSEH LQVSAETIAT IALTCSAYAG
MGDMSITKET FEWALSFPQF NYKNFWFICT ALQRCRIDQA
