ID   FARS_ZEAMM              Reviewed;         534 AA.
AC   C7E5V7;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=(E)-beta-farnesene synthase;
DE            EC=4.2.3.47;
DE   AltName: Full=Terpene synthase 10;
OS   Zea mays subsp. mexicana (Mexican teosinte).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4579;
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; GQ253104; ACT37403.1; -; mRNA.
DR   AlphaFoldDB; C7E5V7; -.
DR   SMR; C7E5V7; -.
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..534
FT                   /note="(E)-beta-farnesene synthase"
FT                   /id="PRO_0000402130"
FT   MOTIF           287..291
FT                   /note="DDXXD motif"
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         431
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         435
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         439
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   534 AA;  61363 MW;  9D2FF64EA44D0DBF CRC64;
     MDATAFHPSL WGDFFVKYKP PTAPKRGHMT ERAELLKEEV RKTLKAAANQ IKNALDLIIT
     LQRLGLDHHY ENEISELLRF VYSSSDYDDK DLYVVSLRFY LLRKHGHCVS SDVFTSFKDE
     EGNFVVDDTK CLLTLYNAAY LRTHGEKVLD EAITFTRRQL EASLLDPLEP ALLADEVSLT
     LQTPLFRRLR ILEAINYIPI YGKEAGRNEA ILELAKLNFN LAQLIYCEEL KEVTLWWKQL
     NVETNLSFIR DRIVECHFWM TGACCEPQYS LSRVIATKMT ALITVLDDMM DTYSTTEEAM
     LLAEAIYGWE ENAAELLPGY MKDFYLYLLK TIDSCGDELG PNRSFRTFYL KEMLKVLVRG
     SSQEIKWRNE NYVPKTISEH LEHSGPSVGA FQVACSSFVG MGDSITKGSF EWLLTYPELA
     KSLMNIARLL NDTASTKREQ NAGHHVSTVQ CYMLMHGTTM DEACEKIKEL TEDSWKDMME
     LYLTPTEHPK LIAQTIVDFA RTADYMYKET DGFTFSHTIK DMIAKLFVDP ISLF