TPS7_RICCO
ID TPS7_RICCO Reviewed; 564 AA.
AC B9RXW0; G5CT99;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Alpha-farnesene synthase;
DE EC=4.2.3.46;
DE AltName: Full=(E,E)-alpha-farnesene synthase;
DE AltName: Full=Terpene synthase 7;
DE Short=RcSeTPS7;
GN Name=TPS7; ORFNames=RCOM_0906600;
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], FUNCTION, AND CATALYTIC ACTIVITY.
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 (E,E)-
CC alpha-farnesene. {ECO:0000269|PubMed:22459969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46;
CC Evidence={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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEF43966.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JN315866; AEQ27768.1; -; mRNA.
DR EMBL; EQ973828; EEF43966.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001310649.1; NM_001323720.1.
DR AlphaFoldDB; B9RXW0; -.
DR SMR; B9RXW0; -.
DR STRING; 3988.XP_002518579.1; -.
DR PRIDE; B9RXW0; -.
DR GeneID; 8267421; -.
DR KEGG; rcu:8267421; -.
DR eggNOG; ENOG502QUXA; Eukaryota.
DR InParanoid; B9RXW0; -.
DR OrthoDB; 401091at2759; -.
DR BRENDA; 4.2.3.46; 1204.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0052578; F:alpha-farnesene synthase activity; IEA:RHEA.
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 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..564
FT /note="Alpha-farnesene synthase"
FT /id="PRO_0000422205"
FT MOTIF 313..317
FT /note="DDXXD motif"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT CONFLICT 136..138
FT /note="AKK -> DVF (in Ref. 1; AEQ27768)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="R -> Q (in Ref. 1; AEQ27768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 65793 MW; F170BA3620A583C8 CRC64;
MKVGQPVLQC QTNSEAFGMM QERRSGNYKP NIWKYDFLQS LSSKYDEEKY KTQAERLKED
AKHLFIEAVD LQGKLELVDC IIKVGLASHF KDEIKKALDT IASSIKNDKS DAIKNRYVTA
LCFRLLRQHG YEVSQAKKSD FLDENGTFLK AKSMDVKGVL ELFEASYLAL ESENILDDAK
AFSTTILKDI NSATTESNLY KQVVHALELP FHWRVRWFDV KWHIKTFQKD KSINKTLLDL
AKVNFNVVQA TLQNDLKEIS RWWRNLGLIE NLKFSRDRLV ESFLCTVGLV FEPQYSSFRR
WLTKVVIMIL VIDDVYDIYG SLEELQHFTN AINRWDTAEL EQLPEYMKIC FKTLHTITGE
TAHEMQREKR WDQEQTETHL KKVWADFCRA LFVEAKWFNK GYTPSVQEYL KTACISSSGS
LLSVHSFFLI MNEGTREMLH FLEKNQEMFY NISLIIRLCN DLGTSVAEQE RGDAASSIVC
HMREMEVLEE EARSYLKGII GNYWKKVNEK CFTQSPEMQL FININVNMAR VVHNLYQNRD
GFGVQDHQNK KQILSLLVHP FKLD
