ID   TPS10_RICCO             Reviewed;         551 AA.
AC   B9T536; G5CTA0;
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=Terpene synthase 10;
DE            Short=RcSeTPS10;
DE            EC=4.2.3.-;
GN   Name=TPS10; ORFNames=RCOM_0766900;
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 [MRNA], AND FUNCTION.
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).
RN   [2]
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).
CC   -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate to
CC       sesquiterpene olefins. {ECO:0000269|PubMed:22459969}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; JN315867; AEQ27769.1; -; mRNA.
DR   EMBL; EQ974507; EEF29028.1; -; Genomic_DNA.
DR   RefSeq; NP_001310631.1; NM_001323702.1.
DR   AlphaFoldDB; B9T536; -.
DR   SMR; B9T536; -.
DR   PRIDE; B9T536; -.
DR   GeneID; 8261702; -.
DR   KEGG; rcu:8261702; -.
DR   eggNOG; ENOG502QUH3; Eukaryota.
DR   InParanoid; B9T536; -.
DR   OrthoDB; 401091at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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   2: Evidence at transcript level;
KW   Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..551
FT                   /note="Terpene synthase 10"
FT                   /id="PRO_0000422208"
FT   MOTIF           303..307
FT                   /note="DDXXD motif"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         455
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        65
FT                   /note="F -> L (in Ref. 1; AEQ27769)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  64630 MW;  9C4EE2AF9D215028 CRC64;
     MTDPIMSNET IIRRSANYRP PIWDFDFVQS LKSEFVGELN IKRIDKLKED VKMMLNKTMA
     PSDQFELIDT LQRLGLAYHF GDEIKRIVKS IYNSHRNDNT WMKEDLHTIA LQFRLLRQHG
     YNISQEIFDI FRDELGNFKE CLHEDIEGML SLYEASYLLE EGENILEVAR EFAASCLKKY
     IQVNKDQLLS MIVSHSLEVP LHWRMPRLET RWFIDIYEKK QGMNPLLLEL AKLDFNNVQA
     TYHEDLKYVT SWWRNTGLGE KLSFARDRLM ENFLWTVGVN FPPQFGYFRR ISTKVNSLIT
     VIDDIYDVYG TLDELQLFTN AVERWDVNAM DQLPEYMKLC FLALHNSINE MAYDALREQG
     FHIIPYLKKA WADLCKSYLV EAKWYYIGYT PTLQEYMDNA WISISAPVIL VHAYFLEGSP
     ITNEALKSLK EYPDIIQWSS MILRFADDLG TSSDELKRGD NPKSIQCYIY ETGVSELKAR
     EHIQYLIGET WKKINKEREY IDSPFSKIFI EVATNLARMA QCMYQHGDGH GIEDGETKDH
     VLSLLVKPIP M