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Database: UniProt
Entry: TPS11_RICCO
LinkDB: TPS11_RICCO
Original site: TPS11_RICCO 
ID   TPS11_RICCO             Reviewed;         572 AA.
AC   B9RHP7;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Probable terpene synthase 11;
DE            Short=RcSeTPS11;
DE            EC=4.2.3.-;
GN   Name=TPS11; ORFNames=RCOM_1764780;
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; EQ973780; EEF49134.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9RHP7; -.
DR   SMR; B9RHP7; -.
DR   STRING; 3988.B9RHP7; -.
DR   eggNOG; ENOG502QW72; Eukaryota.
DR   InParanoid; B9RHP7; -.
DR   OrthoDB; 532254at2759; -.
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; Farnesyl Diphosphate Synthase; 1.
DR   Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 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   PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR31225:SF137; TERPENE SYNTHASE 11-RELATED; 1.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..572
FT                   /note="Probable terpene synthase 11"
FT                   /id="PRO_0000422209"
FT   MOTIF           317..321
FT                   /note="DDXXD motif"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  65426 MW;  73CC61A0201B8606 CRC64;
     MSMIGTKSFF ISSSPKVPVG ISWGPSSYRT NSSLSVRSPT LTCSISTISQ PTRKEPATTK
     PEIMEELHEG TRKELLTSSS PIATMKLIDS IQRLGVGYYF EEEINTLLDR FLDLETTEDL
     LATALRFRLL RDNCFPAHSD VFGKFMNKDG KFKESLRKDV WGLLSLYEAS YLGTKDEVEL
     VEAMEFTKTC LEEQSIPLMA HKLSRHVSQA LDLPRHLRMP RLEARNYIHE YSLESNNSPP
     LLELAKLEFN AVQSLHQKEL IEIVRWWKQL GLVDKLGFAR DRPLECYLWT VGIFPEPYNS
     TCRIELTKTI AILLVIDDIF DTYGSLPDLI LFTEAVRRWD LNAMESLPEY MKICYMALYN
     TTNDIGFMIL KRHGLSIVPH LKRTWIDMFE AFLTEAKWFN SGYVPTLEEY LDNGVTTGGT
     YMALVHSFFL MGQGVNKETV TMMEPYPDLF SLSGRILRLW DDLGTAREEQ ERGDVACSIE
     CLMREKRISC DDEGRKQVRQ LIRSLWTELN GELIAPSAMP LSIINASLNL ARTAQVVYQH
     GDDKKGSSVD NQVQALIYIP ISFPKRRDLK LL
//
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