ID   FARS_CITJU              Reviewed;         560 AA.
AC   Q94JS8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=(E)-beta-farnesene synthase;
DE            Short=CjFS;
DE            EC=4.2.3.47;
DE   AltName: Full=Terpene synthase 10;
OS   Citrus junos (Yuzu) (Citrus ichangensis x Citrus reticulata var. austera).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=135197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11642326; DOI=10.1248/bpb.24.1171;
RA   Maruyama T., Ito M., Honda G.;
RT   "Molecular cloning, functional expression and characterization of (E)-beta
RT   farnesene synthase from Citrus junos.";
RL   Biol. Pharm. Bull. 24:1171-1175(2001).
CC   -!- FUNCTION: Sesquiterpene cyclase catalyzing the production of beta-
CC       farnesene from farnesyl diphosphate. {ECO:0000269|PubMed:11642326}.
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:11642326};
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; AF374462; AAK54279.1; -; mRNA.
DR   AlphaFoldDB; Q94JS8; -.
DR   SMR; Q94JS8; -.
DR   KEGG; ag:AAK54279; -.
DR   BioCyc; MetaCyc:MON-13547; -.
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: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.
FT   CHAIN           1..560
FT                   /note="(E)-beta-farnesene synthase"
FT                   /id="PRO_0000402129"
FT   MOTIF           312..316
FT                   /note="DDXXD motif"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         457
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   560 AA;  64223 MW;  89742075BBB4A317 CRC64;
     MKDMSIPLLA AVSSSTEETV RPIADFHPTL WGNHFLKSAA DVETIDAATQ EQHAALKQEV
     RRMITTTANK LAQKLHMIDA VQRLGVAYHF EKEIEDELGK VSHDLDSDDL YVVSLRFRLF
     RQQGVKISCD VFDKFKDDEG KFKESLINDI RGMLSLYEAA YLAIRGEDIL DEAIVFTTTH
     LKSVISISDH SHANSNLAEQ IRHSLQIPLR KAAARLEARY FLDIYSRDDL HDETLLKFAK
     LDFNILQAAH QKEASIMTRW WNDLGFPKKV PYARDRIIET YIWMLLGVSY EPNLAFGRIF
     ASKVVCMITT IDDTFDAYGT FEELTLFTEA VTRWDIGLID TLPEYMKFIV KALLDIYREA
     EEELAKEGRS YGIPYAKQMM QELIILYFTE AKWLYKGYVP TFDEYKSVAL RSIGLRTLAV
     ASFVDLGDFI ATKDNFECIL KNAKSLKATE TIGRLMDDIA GYKFEQKRGH NPSAVECYKN
     QHGVSEEEAV KELLLEVANS WKDINEELLN PTTVPLPMLQ RLLYFARSGH FIYDDGHDRY
     THSLMMKRQV ALLLTEPLAI