ID   FARS_ZEAMH              Reviewed;         533 AA.
AC   C7E5V8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=(E)-beta-farnesene synthase;
DE            EC=4.2.3.47;
DE   AltName: Full=Terpene synthase 10;
OS   Zea mays subsp. huehuetenangensis (San Antonio Huista teosinte).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=112001;
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 beta-
CC       farnesene and alpha-bergamotene in equal amounts from farnesyl
CC       diphosphate. Involved in indirect defense by producing volatile signals
CC       attracting natural enemies of herbivores.
CC       {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; GQ253105; ACT37404.1; -; mRNA.
DR   AlphaFoldDB; C7E5V8; -.
DR   SMR; C7E5V8; -.
DR   BRENDA; 4.2.3.47; 6752.
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_0000402131"
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;  61432 MW;  A9261D3F88E39D0D CRC64;
     MDATAFHPSL WGDFFVKYKP PTAPKRGHMT ERAELLKEEV RKTLKAAANQ IKNALDLIIT
     LQRLGLDHHY ENEISELLRF VYSSSDYDDK DLYVVSLRFY LLRKHGHCVS SDVFTSFKDE
     EGNFVVDDTK CLLSLYNAAY FRTHGEKVLD EAIAFTRRQL EASLLDPLEP ALADEVHLTL
     QTPLFRRLRI LEAINYIPIY GKEAGRNEAI LELAKLNFNL AQLIYCGELK EVTLWWKQLN
     VETNLSFIRD RIVECHFWMT GACCEPQYSL SRVIATKMTA LITVLDDMMD TYSTTEEAML
     LAEAIYRWEE NAAELLPGYM KDFYLYLLKT IDSCGDELGP NRSFRTFYLK EMLKVLVRGS
     SQEIKWRNEN YVPKTISEHL EHSGPTVGAF QVACSSFVGM GDIITKESFE WLLTYPELVK
     SLMNIARLLN DTASTKREQN AGQHVSTVQC YMLKHGTTMD EACEKVKELT EDSWKDMMEL
     YLTPTEHPKL IAQTIVDFAR TADYMYKETD GFTFSHTIKD MIAKLFVDPI SLF