ID   TPS2_RICCO              Reviewed;         550 AA.
AC   B9SCB6;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable terpene synthase 2;
DE            Short=RcSeTPS2;
DE            EC=4.2.3.-;
GN   Name=TPS2; ORFNames=RCOM_0890850;
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; EQ973920; EEF38721.1; -; Genomic_DNA.
DR   RefSeq; XP_002523635.1; XM_002523589.1.
DR   AlphaFoldDB; B9SCB6; -.
DR   SMR; B9SCB6; -.
DR   STRING; 3988.XP_002523635.1; -.
DR   PRIDE; B9SCB6; -.
DR   GeneID; 8289511; -.
DR   KEGG; rcu:8289511; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   InParanoid; B9SCB6; -.
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..550
FT                   /note="Probable terpene synthase 2"
FT                   /id="PRO_0000422200"
FT   MOTIF           305..309
FT                   /note="DDXXD motif"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  63680 MW;  219AFABAE46B64BC CRC64;
     MSAQTLAISN LKPNTTRHLA SFHPNIWGDR FLSCAAESTD IEDDMEQQVE RLKEEVKKMI
     ASADEPSQIL NLIDLLQRLG VSYHFEKEIE EALQQVLNMN SDSDKDDDLH SVALRFRLLR
     EQGLNVSCDV FNKFRDRNGH FIQTLKTDLQ GMLSLYEAAH FRVHGEGILD DALAFTTTYL
     ESIVPNLSPP LAAQISRTLR QPLRKSLARV EARHFISIYQ EDTSHNEVLL TFAKLDFNLL
     QKLHQKELKY ISLWWKDLDF VNKLPFTRDR VVEGYFWILG VYFEPQYHRA RKFVTKVINV
     VSVIDDIYDA YGTLEELVVF TDAINRWDID CIDQLPEYMK VCYKALLNVY EEIERALSEQ
     GRSYRLHYAK EAMKKLVQAY LVEANWMNKN YVPTMDEYMS IALVSCAYPL LTVTSFVGMG
     DIATKEVFDW ASNDPKIVRV ASIICRLMDD IVSHEFEQKR GHIASSVECY MKQNGVSEEA
     TRDEFNKQIV DAWKDINEEH LQPNYVPMPF RTRVVNSARI MDYLYKDDDE YTHVGELMKG
     SVAALLIDPA