ID   TPS4_RICCO              Reviewed;         563 AA.
AC   B9RHX7;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Probable terpene synthase 4;
DE            Short=RcSeTPS4;
DE            EC=4.2.3.-;
GN   Name=TPS4; ORFNames=RCOM_1574410;
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; EEF48749.1; -; Genomic_DNA.
DR   RefSeq; XP_002513346.1; XM_002513300.1.
DR   AlphaFoldDB; B9RHX7; -.
DR   SMR; B9RHX7; -.
DR   STRING; 3988.XP_002513346.1; -.
DR   PRIDE; B9RHX7; -.
DR   GeneID; 8259987; -.
DR   KEGG; rcu:8259987; -.
DR   eggNOG; ENOG502QTGK; Eukaryota.
DR   InParanoid; B9RHX7; -.
DR   OrthoDB; 449049at2759; -.
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..563
FT                   /note="Probable terpene synthase 4"
FT                   /id="PRO_0000422202"
FT   MOTIF           316..320
FT                   /note="DDXXD motif"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
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   563 AA;  64489 MW;  E55F1841EF5C675F CRC64;
     MANAISNPAS FIGVHSPIAQ IRIPRLCVAK GMPTPIAQRD IILQDQIQLE NTCIRHAKAL
     KEARLAFSKV RKDHSQNLIM IDALQRLGID YHFQEETQDV LEGQYNKIFA AHQQHHLSDA
     ALRFRLLRQQ GYYVPASDVF SELKNREGKF KQELAADIKG LMELYEASQL SIQEENILDE
     AGAFSAHFLN CWTPHLCDHQ TRIVSNTLKH PFHRTLARST IKNFLHFYNF QGENEYIQTF
     TELAKLDFNM IQSIHRQEIN QVSNWWNNLG LASELKFARD QPEKWCMWPL VGVTDPSLSW
     QRIELAKPVS LVYLIDDIFD LGGTPDQLTL FTEAVNRWEI TATEDLPYHM KICFRALYDV
     TNQIAYKVYK KHQYNPIHSL KKAWARLCNA FLEEAKWFAA GKLPKADEYL NTAIVTSGVH
     LVLVHTFFLM GDGITDQTIN LLNNDDPGII SSVATILRLW DDLGSAQDEN QDGYDGSYIE
     CYMKDFPGTS VRDARNHVIS MISDTWKKLN QHCLSPNPFS GSFIRATLNG ARMVPLMYDF
     DSNHNLPILQ QNIKSLLFES VAI