ID   TPS6_RICCO              Reviewed;         555 AA.
AC   B9RI00;
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 6;
DE            Short=RcSeTPS6;
DE            EC=4.2.3.-;
GN   Name=TPS6; ORFNames=RCOM_1574750;
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; EQ973781; EEF48772.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9RI00; -.
DR   SMR; B9RI00; -.
DR   STRING; 3988.XP_002513369.1; -.
DR   PRIDE; B9RI00; -.
DR   eggNOG; ENOG502SHPY; Eukaryota.
DR   InParanoid; B9RI00; -.
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..555
FT                   /note="Probable terpene synthase 6"
FT                   /id="PRO_0000422204"
FT   MOTIF           309..313
FT                   /note="DDXXD motif"
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         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  64359 MW;  5CDC9EDEF03FD55E CRC64;
     MAEKDKYRPL ANFPSTAWGC SFASFSSSNS DFELYTREVE TLKEKVRPMV TASTKDPLEN
     VQIINLLYRL GVSYHFENEI TDQLNHIFEI IPNHIISDDN DYDLYTVAIL FQILRQYGHK
     VPCDVFNKFK NSDGKFKKSI ANDLKGLLSL YEASFLSVHG ENILDEAIAF TRPLLESFAD
     QSSPHLAKYI RNSLLRPHHQ GIQRVEARQY ISFYEEDESR NETLLKFAKL DFNRLQLLHK
     QELASLSRYK KYIAQIIIWE DLNLAKELPY IRDRLVETYL WAIGAHFEPQ YALSRAIIAK
     YTTIVSAVDD TYDAYGTLDE LQRFTNAFQR CDIDAIDELP DYMKVLYRAL LNFFDQIEDE
     VDEGRSYSTS VAKEAFKELV RSYYVEAQWF SDGYVPSFDE YMRNGLITST YTVLPAASFI
     GMENTVGEKE YKWVQSNPKI VKAAKIICRL MDDITTHEDE QKRGHCASSI ECYMKEYGVS
     EKKAIEEIQK ICANAWKDMN EECMKKPPTV SRTLLKYYVN LARVIDFVYK NLDSYTYASS
     LKGDITTVFL ELLPV