ID   TPS3_RICCO              Reviewed;         547 AA.
AC   B9SBV6;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Probable terpene synthase 3;
DE            Short=RcSeTPS3;
DE            EC=4.2.3.-;
GN   Name=TPS3; ORFNames=RCOM_1045160;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale;
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
RN   [2]
RP   GENE NAME.
RX   PubMed=22459969; DOI=10.1016/j.phytochem.2012.02.022;
RA   Xie X., Kirby J., Keasling J.D.;
RT   "Functional characterization of four sesquiterpene synthases from Ricinus
RT   communis (castor bean).";
RL   Phytochemistry 78:20-28(2012).
CC   -!- FUNCTION: Probable sesquiterpene synthase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
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}.
CC   -!- MISCELLANEOUS: Does not produce any detectable product when tested in
CC       vitro. {ECO:0000305|PubMed:22459969}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; EQ973917; EEF38934.1; -; Genomic_DNA.
DR   RefSeq; XP_002523475.1; XM_002523429.2.
DR   AlphaFoldDB; B9SBV6; -.
DR   SMR; B9SBV6; -.
DR   STRING; 3988.XP_002523475.1; -.
DR   PRIDE; B9SBV6; -.
DR   GeneID; 8282483; -.
DR   KEGG; rcu:8282483; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   InParanoid; B9SBV6; -.
DR   OrthoDB; 360509at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
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:0120251; P:hydrocarbon biosynthetic process; 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   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..547
FT                   /note="Probable terpene synthase 3"
FT                   /id="PRO_0000422201"
FT   MOTIF           298..302
FT                   /note="DDXXD motif"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   547 AA;  63693 MW;  1BB11051F0B3DFAC CRC64;
     MALPVQAAPQ RAQVRRTAQF HPSVWGDYFI KNAPDNKMVS IWKEQAKVLE EEVRRMIISE
     TQKPSGKLKL IDVIQRLGIA YHFEEEIGEV IEQVYSNYDD DEDLYDIALR FRLLRQQGYN
     VSSDVFDKFK DCKGDFKKHL VNDVQGLLSL HEASYMSVQG EKILDEALEF TKTHLMATQL
     SSPLPDQVSH ALRWPVRRGL PRKEAWQYFS IYQQDREHIE PLLKLAKLDF NIVQKLHHKD
     MSIITRWWID LDFTTKLSFA RDRVIECSFW ALGVFYEPQF VFARQVLSKA VAILSVMDDI
     YDVHGTIEEL ELFTEVVERW DISMKDQLPD YMKWYFEALI DFYAEIEAET TKGGRSFCIH
     YAKEAVKKQV RAYITEARWF NNDYVPTLEE YISNAVISST YPILITLSFC GMGKFASKDV
     FDWLFTEPNK LLYTASGLAR LIDDIRSHEF EQERGHVASA VECYMKQHSV SKQEAYNELN
     SIVVNMWKDL NEELLKETGV LPKPILACIL NIVRVMDVVY KDEDSYTNSR NSLKDILATF
     LVNPVPV