ID   FARS_ZEAPE              Reviewed;         533 AA.
AC   C7E5W0;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=(E)-beta-farnesene synthase;
DE            EC=4.2.3.47;
DE   AltName: Full=Terpene synthase 10;
OS   Zea perennis (Perennial teosinte) (Euchlaena perennis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19646721; DOI=10.1016/j.phytochem.2009.06.011;
RA   Koellner T.G., Gershenzon J., Degenhardt J.;
RT   "Molecular and biochemical evolution of maize terpene synthase 10, an
RT   enzyme of indirect defense.";
RL   Phytochemistry 70:1139-1145(2009).
CC   -!- FUNCTION: Sesquiterpene cyclase catalyzing the production of sixfold
CC       more beta-farnesene than alpha-bergamotene from farnesyl diphosphate.
CC       Involved in indirect defense by producing volatile signals attracting
CC       natural enemies of herbivores. {ECO:0000269|PubMed:19646721}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC         diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC         Evidence={ECO:0000269|PubMed:19646721};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; GQ253107; ACT37406.1; -; mRNA.
DR   AlphaFoldDB; C7E5W0; -.
DR   SMR; C7E5W0; -.
DR   BRENDA; 4.2.3.47; 11311.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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   Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Plant defense.
FT   CHAIN           1..533
FT                   /note="(E)-beta-farnesene synthase"
FT                   /id="PRO_0000402133"
FT   MOTIF           286..290
FT                   /note="DDXXD motif"
FT   BINDING         286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         430
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         434
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   533 AA;  61619 MW;  AB61BE74C0ED2574 CRC64;
     MDATAFHPSL WGDFFVKYEP PTAPKRGHMT QRAELLKEEV RKTLKAAANQ IKNALDLIIT
     LQRLGLDHHY ENEISELLRF VYSSSDYDDK DLYVVSLRFY LLRKHGHRVS SDVFMSFKDE
     EGNFVVDDTK CLLSLYNAAY LMTHGEKVLD EAITFTRRQL EALLLDPLEP ALADEVYLTL
     QTPLFRRLRI LEAVNYIPIY GKEAGRNEAI LELAKLNFNL AQLIYCEELK EVTLWWKQLN
     VETNLSFIRD RIVECHFWMT GACCEPRYSL SRVIATKMTA LITVLDDMMD TYSTTEEAML
     LAEAIYRWEE NAAELLPGYM KHFYLYLLKT IDSCGGELGP NRSFRTFYLK EMLKVFVRGS
     SQEIKWRNEN YVPKTISEHL EHSGPTVGAF QVACSSFVGM GDNITKESFE WLLTYPELVK
     SLMNIARLLN DTASTKREQT AGHHVSTVQC YMLKHGTTMD EACEKIKELT EDSWKDMMEL
     YLTPTEHPKL VAQTIVDFAR TADYMYKETD GFTFSHTIKD MIAKLFVDPI SLF