ID   TPS9_RICCO              Reviewed;         584 AA.
AC   B9RPM3;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Probable terpene synthase 9;
DE            Short=RcSeTPS9;
DE            EC=4.2.3.-;
GN   Name=TPS9; ORFNames=RCOM_1545320;
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; EQ973796; EEF46639.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9RPM3; -.
DR   SMR; B9RPM3; -.
DR   PRIDE; B9RPM3; -.
DR   eggNOG; ENOG502QUH3; Eukaryota.
DR   InParanoid; B9RPM3; -.
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..584
FT                   /note="Probable terpene synthase 9"
FT                   /id="PRO_0000422207"
FT   MOTIF           339..343
FT                   /note="DDXXD motif"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   584 AA;  67734 MW;  FF7B9D21AE932DAB CRC64;
     MEIVFSSSLS STLTVTKILR SPRHATTGNM QDYSRFPLFF TIASRSNASQ AKHRRSANYH
     PTIWDPKAIE CLRTPYTYDG VHGARLQKLK DEVRSLLTTF TKEPCGQLKL IDSMQRLGVS
     YHFREEIEEI LNLVELDSDS DLYTTALHFR LLRQHGFTIS KEVFEKFRNE DGKFKDSLKE
     DILGLLSLYD ASYLGMHGEH ILEEAKDFST EQLKSLLGRS QGDIVTYQVK QALDVPLHWR
     MQRIENRNYI NIYQKEDTNN LALLELAKLD YNLVQSVYQI ELKELARWWI ALGFREKLHF
     SRDRLMENYL WSMGMIFEPH FSKCRIYLTK FICILSSIDD MYDIYGSLDE LELFTSALKR
     WDPMALEELP DYMKICYLAI LNFASELVYD VLKEEGLYTL PFIRDEWVKL CQAYLVEARW
     FNSGYTPTFD EYLENAWISV GGHEAIVHAC ALLGHTSTED FQNFLKHGFE LIYWSSLLVR
     LNDDLGTSQA EIKRGDVVKS IQCYMIEKGV SEKEAKDHVK GLISHAWKVL NEESVKCSLS
     RSFVNVCLNM TRTAQCIFQY GDGIGTSIGV TKDRLEFLIV KPIL