FARS_MAIZE
ID FARS_MAIZE Reviewed; 533 AA.
AC Q2NM15; Q2NM14;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=(E)-beta-farnesene synthase {ECO:0000303|PubMed:19646721};
DE EC=4.2.3.47 {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721, ECO:0000269|PubMed:21607717};
DE AltName: Full=(+)-germacrene D synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.77 {ECO:0000269|PubMed:16418295};
DE AltName: Full=(E)-alpha-bergamotene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.81 {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721, ECO:0000269|PubMed:21607717};
DE AltName: Full=Alpha-copaene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.133 {ECO:0000269|PubMed:16418295};
DE AltName: Full=Alpha-muurolene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.125 {ECO:0000269|PubMed:16418295};
DE AltName: Full=Beta-bisabolene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.55 {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
DE AltName: Full=Beta-caryophyllene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.57 {ECO:0000269|PubMed:16418295};
DE AltName: Full=Delta-cadinene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.- {ECO:0000269|PubMed:16418295};
DE AltName: Full=Sesquiphellandrene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.123 {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
DE AltName: Full=Sesquisabinene A synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.- {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
DE AltName: Full=Terpene synthase 10 {ECO:0000303|PubMed:19646721};
DE AltName: Full=Zingiberene synthase {ECO:0000303|PubMed:16418295};
DE EC=4.2.3.65 {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
GN Name=TPS10 {ECO:0000303|PubMed:19646721};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY HERBIVORY, AND PATHWAY.
RC STRAIN=cv. B73, and cv. Delprim;
RX PubMed=16418295; DOI=10.1073/pnas.0508027103;
RA Schnee C., Koellner T.G., Held M., Turlings T.C., Gershenzon J.,
RA Degenhardt J.;
RT "The products of a single maize sesquiterpene synthase form a volatile
RT defense signal that attracts natural enemies of maize herbivores.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1129-1134(2006).
RN [2]
RP INDUCTION BY HERBIVORES.
RC STRAIN=cv. B73;
RX PubMed=18296628; DOI=10.1105/tpc.107.051672;
RA Koellner T.G.J., Held M., Lenk C., Hiltpold I., Turlings T.C.,
RA Gershenzon J., Degenhardt J.;
RT "A maize (E)-beta-caryophyllene synthase implicated in indirect defense
RT responses against herbivores is not expressed in most American maize
RT varieties.";
RL Plant Cell 20:482-494(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-356, AND PATHWAY.
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).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21607717; DOI=10.1007/s10886-011-9967-7;
RA Fontana A., Held M., Fantaye C.A., Turlings T.C., Degenhardt J.,
RA Gershenzon J.;
RT "Attractiveness of constitutive and herbivore-induced sesquiterpene blends
RT of maize to the parasitic wasp Cotesia marginiventris (Cresson).";
RL J. Chem. Ecol. 37:582-591(2011).
RN [5]
RP REVIEW.
RX PubMed=30187155; DOI=10.1007/s00425-018-2999-2;
RA Block A.K., Vaughan M.M., Schmelz E.A., Christensen S.A.;
RT "Biosynthesis and function of terpenoid defense compounds in maize (Zea
RT mays).";
RL Planta 249:21-30(2019).
CC -!- FUNCTION: Sesquiterpene cyclase catalyzing mainly the production of
CC beta-farnesene and alpha-bergamotene in equal amounts from farnesyl
CC diphosphate (PubMed:19646721, PubMed:16418295, PubMed:21607717).
CC Mediates also the biosynthesis of minor sesquiterpene hydrocarbons
CC including alpha-muurolene, beta-bisabolene, zingiberene,
CC sesquiphellandrene, sesquisabinene A, germacrene D, delta-cadinene,
CC alpha-copaene and (E)-beta-caryophyllene (PubMed:16418295,
CC PubMed:19646721). Involved in indirect defense by producing volatile
CC signals attracting natural enemies of herbivores (PubMed:19646721,
CC PubMed:16418295, PubMed:21607717). {ECO:0000269|PubMed:16418295,
CC ECO:0000269|PubMed:19646721, ECO:0000269|PubMed:21607717}.
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:16418295, ECO:0000269|PubMed:19646721,
CC ECO:0000269|PubMed:21607717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721,
CC ECO:0000269|PubMed:21607717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate;
CC Xref=Rhea:RHEA:33991, ChEBI:CHEBI:10221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.133;
CC Evidence={ECO:0000269|PubMed:16418295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33992;
CC Evidence={ECO:0000269|PubMed:16418295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene +
CC diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62756, ChEBI:CHEBI:175763; EC=4.2.3.81;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721,
CC ECO:0000269|PubMed:21607717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31428;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721,
CC ECO:0000269|PubMed:21607717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:16418295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:16418295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate;
CC Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:16418295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557;
CC Evidence={ECO:0000269|PubMed:16418295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate;
CC Xref=Rhea:RHEA:30427, ChEBI:CHEBI:33019, ChEBI:CHEBI:49046,
CC ChEBI:CHEBI:175763; EC=4.2.3.77;
CC Evidence={ECO:0000269|PubMed:16418295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30428;
CC Evidence={ECO:0000269|PubMed:16418295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-zingiberene +
CC diphosphate; Xref=Rhea:RHEA:28643, ChEBI:CHEBI:10115,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.65;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28644;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate;
CC Xref=Rhea:RHEA:33103, ChEBI:CHEBI:33019, ChEBI:CHEBI:64797,
CC ChEBI:CHEBI:175763; EC=4.2.3.125;
CC Evidence={ECO:0000269|PubMed:16418295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33104;
CC Evidence={ECO:0000269|PubMed:16418295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:28266, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49263, ChEBI:CHEBI:175763; EC=4.2.3.55;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28267;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-sesquiphellandrene +
CC diphosphate; Xref=Rhea:RHEA:32699, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:64361, ChEBI:CHEBI:175763; EC=4.2.3.123;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32700;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + sesquisabinene A;
CC Xref=Rhea:RHEA:60020, ChEBI:CHEBI:33019, ChEBI:CHEBI:143551,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:16418295,
CC ECO:0000269|PubMed:19646721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60021;
CC Evidence={ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q6JD73};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q6JD73};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q5GJ60};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:19646721,
CC ECO:0000269|PubMed:21607717, ECO:0000305|PubMed:30187155}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC -!- INDUCTION: Induced in leaves by herbivory (e.g. S.littoralis).
CC {ECO:0000269|PubMed:16418295, ECO:0000269|PubMed:18296628}.
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 {ECO:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AY928078; AAX99146.1; -; mRNA.
DR EMBL; AY928079; AAX99147.1; -; mRNA.
DR RefSeq; NP_001105850.2; NM_001112380.2.
DR AlphaFoldDB; Q2NM15; -.
DR SMR; Q2NM15; -.
DR STRING; 4577.GRMZM2G179092_P01; -.
DR PaxDb; Q2NM15; -.
DR PRIDE; Q2NM15; -.
DR EnsemblPlants; Zm00001eb415160_T001; Zm00001eb415160_P001; Zm00001eb415160.
DR GeneID; 732751; -.
DR Gramene; Zm00001eb415160_T001; Zm00001eb415160_P001; Zm00001eb415160.
DR KEGG; zma:732751; -.
DR MaizeGDB; 1219901; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:MON-12833; -.
DR BRENDA; 4.2.3.47; 6752.
DR BRENDA; 4.2.3.81; 6752.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; Q2NM15; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102884; F:alpha-zingiberene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102887; F:beta-sesquiphellandrene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; 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;
KW Reference proteome.
FT CHAIN 1..533
FT /note="(E)-beta-farnesene synthase"
FT /id="PRO_0000402134"
FT MOTIF 286..290
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
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 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
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 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
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 430
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT VARIANT 52
FT /note="T -> K (in strain: cv. Delprim)"
FT VARIANT 134
FT /note="S -> T (in strain: cv. Delprim)"
FT VARIANT 141..144
FT /note="VRTH -> LRTQ (in strain: cv. Delprim)"
FT VARIANT 171
FT /note="A -> AL (in strain: cv. Delprim)"
FT VARIANT 177
FT /note="H -> S (in strain: cv. Delprim)"
FT MUTAGEN 356
FT /note="L->F: Decreased production of alpha-bergamotene."
FT /evidence="ECO:0000269|PubMed:19646721"
SQ SEQUENCE 533 AA; 61534 MW; AB695CFF3A2AA979 CRC64;
MDATAFHPSL WGDFFVKYKP PTAPKRGHMT ERAELLKEEV RKTLKAAANQ ITNALDLIIT
LQRLGLDHHY ENEISELLRF VYSSSDYDDK DLYVVSLRFY LLRKHGHCVS SDVFTSFKDE
EGNFVVDDTK CLLSLYNAAY VRTHGEKVLD EAITFTRRQL EASLLDPLEP ALADEVHLTL
QTPLFRRLRI LEAINYIPIY GKEAGRNEAI LELAKLNFNL AQLIYCEELK EVTLWWKQLN
VETNLSFIRD RIVECHFWMT GACCEPQYSL SRVIATKMTA LITVLDDMMD TYSTTEEAML
LAEAIYRWEE NAAELLPRYM KDFYLYLLKT IDSCGDELGP NRSFRTFYLK EMLKVLVRGS
SQEIKWRNEN YVPKTISEHL EHSGPTVGAF QVACSSFVGM GDSITKESFE WLLTYPELAK
SLMNISRLLN DTASTKREQN AGQHVSTVQC YMLKHGTTMD EACEKIKELT EDSWKDMMEL
YLTPTEHPKL IAQTIVDFAR TADYMYKETD GFTFSHTIKD MIAKLFVDPI SLF
