TPS5B_MAIZE
ID TPS5B_MAIZE Reviewed; 554 AA.
AC Q6JD69;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Inactive sesquithujene synthase B {ECO:0000303|PubMed:15075399};
DE AltName: Full=Terpene synthase 5 {ECO:0000303|PubMed:15075399};
DE Short=tps5-Del2 {ECO:0000303|PubMed:15075399};
GN Name=TPS5B {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], AND FUNCTION.
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 having less than 1% of
CC the activity found in TPS5A. {ECO:0000269|PubMed:15075399}.
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; AY518314; AAS88575.1; -; mRNA.
DR AlphaFoldDB; Q6JD69; -.
DR SMR; Q6JD69; -.
DR PRIDE; Q6JD69; -.
DR MaizeGDB; 1219892; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q6JD69; 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 2: Evidence at transcript level;
KW Cytoplasm; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..554
FT /note="Inactive sesquithujene synthase B"
FT /id="PRO_0000418852"
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"
SQ SEQUENCE 554 AA; 63811 MW; 2E2BD1BB93F56F59 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 LQVSAESIGA NALTCSAYAG
MGDMSITKET FEWALSFPQF IRTFGSFVRL SNDVVSTKRE QTKDHSPSTV HCYMKEHGIT
MDDACEKIKE LIEDSWKDML EQSLALKGLP KVVPQLVFDF SRTTDNMYRD RDALTSSEAL
KEMIQLLFVE PIPE
