ID   TPS12_RICCO             Reviewed;         587 AA.
AC   B9T825;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable terpene synthase 12;
DE            Short=RcSeTPS12;
DE            EC=4.2.3.-;
GN   Name=TPS12; ORFNames=RCOM_0058130;
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; EQ974896; EEF27987.1; -; Genomic_DNA.
DR   RefSeq; XP_002534394.1; XM_002534348.1.
DR   AlphaFoldDB; B9T825; -.
DR   SMR; B9T825; -.
DR   STRING; 3988.XP_002534394.1; -.
DR   PRIDE; B9T825; -.
DR   GeneID; 8260996; -.
DR   KEGG; rcu:8260996; -.
DR   eggNOG; ENOG502QUH3; Eukaryota.
DR   InParanoid; B9T825; -.
DR   OrthoDB; 401091at2759; -.
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..587
FT                   /note="Probable terpene synthase 12"
FT                   /id="PRO_0000422210"
FT   MOTIF           338..342
FT                   /note="DDXXD motif"
FT   BINDING         338
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   587 AA;  67929 MW;  25C62D02BACAAB1A CRC64;
     MAINLFKVSN FYTMRSYVSP HVPVPNVNLQ SVSCSAKAEL PHLRPVIKRR SANYPPTIWT
     YNFVQSLNNH NADVLYKEKA RKLEEEVRRL INNESQEMLT TLELIDGIQR LGLAYLFEKD
     IKGALDRFVS MGGCHVLPRK SLHAIALSFR LLRQHGYEVY QDDFKDFMDQ KGELLKCFKK
     DVQGILSFYE ASFCNLEGED LLEKAKTETK VYLNDLQRNS KSDTVESISH ALELPLCRRM
     VMLEARWYIE AYNKREDSNY TLLELAKLNF NMAQSILQRD LKDMSRWWNN LGLANKLSFS
     RDRLMECFFW TIGMAFEPQF SSCRKGLTKV TSLITTIDDV YDVYGTLDEL EVFTDAVERW
     DVNAVRDLPN CMQLSFLALY NTINEMAYET LKEQGEHIIP YLTKAWADLC KAFLQEARWS
     HSKCIPSFDD YVENGWRSAS GNVILVHAYF LLGHNSKQAL DSLLNYHDIL RWPSVVFRLC
     NDLATSSDEL NRGETANSIS CYMFENRVSE EQAREQINKL IDKAWTKMNE YHIGATHFGE
     PFIEAAINVA RIPQCIYRHG DDHGAPDSRS KERVWSLIIE SISLVDS