FARS_ZEADI
ID FARS_ZEADI Reviewed; 533 AA.
AC C7E5V9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=(E)-beta-farnesene synthase;
DE EC=4.2.3.47;
DE AltName: Full=Terpene synthase 10;
OS Zea diploperennis (Diploperennial teosinte).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4576;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF PHE-356.
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; GQ253106; ACT37405.1; -; mRNA.
DR AlphaFoldDB; C7E5V9; -.
DR SMR; C7E5V9; -.
DR BRENDA; 4.2.3.47; 6750.
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_0000402132"
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"
FT MUTAGEN 356
FT /note="F->L: Decreased production of beta-farnesene and
FT increased production of alpha-bergamotene."
FT /evidence="ECO:0000269|PubMed:19646721"
SQ SEQUENCE 533 AA; 61532 MW; 9B7CD1BFDC850BF4 CRC64;
MDATAFHPSL WGDFFVKYKP PTAPKRGHMT QRAELLKEEV RKTLKAAANQ IKNALDLIIT
LQRLGLDHHY ENEISELLRF VYSSSDYDDK DLYVVSLRFY LLRKHGHCVS SDVFTSFKDE
EGNFVVDDTK CLLSLYNAAY LRTHGEKVLD EAITFTRRQL EALLLDSLEP ALADEVHLTL
QTPLFRRLRI LEAVNYIPIY GKEAGRNEAI LELAKLNFNL AQLIYCEELK EITLWWKQLN
VETNLSFIRD RIVECHFWMT GACCEPQYSL SRVIATKMTA LITVLDDMMD TYSTTEEAML
LAEAIYRWEE SAAELLPGYM KDFYLYLLKT IDSCGDELGP NRSFRTFYLK EMLKVFVRGS
SQEIKWRNEN YVPKTISEHL EHSGPTVGAF QVACSSFVGM GDNITKESFE WLLTYPELVK
SLMNIARLLN DTASTKREQN AGHHVSTVQC YMLKHGTTMD EACDKIKELT EDSWKDMMEL
YLTPTEHPKL IAQTIVDFAR TADYMYKETD GFTFSHTIKD MIAKLFVDPI SLF
