TPSBF_MENPI
ID TPSBF_MENPI Reviewed; 550 AA.
AC O48935; Q5W282;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Beta-farnesene synthase;
DE EC=4.2.3.47;
OS Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC Mentha.
OX NCBI_TaxID=34256;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=cv. Black Mitcham; TISSUE=Oil gland;
RX PubMed=9371761; DOI=10.1073/pnas.94.24.12833;
RA Crock J., Wildung M., Croteau R.;
RT "Isolation and bacterial expression of a sesquiterpene synthase cDNA clone
RT from peppermint (Mentha x piperita, L.) that produces the aphid alarm
RT pheromone (E)-beta-farnesene.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12833-12838(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS OF LEU-471 AND
RP SER-531, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Leaf;
RX PubMed=16083926; DOI=10.1016/j.phytochem.2005.06.012;
RA Prosser I.M., Adams R.J., Beale M.H., Hawkins N.D., Phillips A.L.,
RA Pickett J.A., Field L.M.;
RT "Cloning and functional characterisation of a cis-muuroladiene synthase
RT from black peppermint (Menthaxpiperita) and direct evidence for a chemotype
RT unable to synthesise farnesene.";
RL Phytochemistry 67:1564-1571(2006).
CC -!- FUNCTION: Involved in the production of (E)-beta-farnesene, an aphid
CC alarm pheromone. Can use both farnesyl diphosphate and geranyl
CC diphosphate as substrate, but not geranylgeranyl diphosphate. Produces
CC mainly (E)-beta-farnesene, but also smaller amounts of (Z)-beta-
CC farnesene and gamma-cadinene when used with farnesyl diphosphate as
CC substrate. In the presence of geranyl diphosphate, produces limonene,
CC terpinolene and the acyclic monoterpene myrcene along with minor
CC amounts of gamma-terpinene, (Z)-ocimene, (E)-ocimene and sabinene.
CC {ECO:0000269|PubMed:9371761}.
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:16083926, ECO:0000269|PubMed:9371761};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:9371761};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:9371761};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000305|PubMed:9371761};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for farnesyl diphosphate {ECO:0000269|PubMed:16083926,
CC ECO:0000269|PubMed:9371761};
CC KM=1.5 uM for geranyl diphosphate {ECO:0000269|PubMed:16083926,
CC ECO:0000269|PubMed:9371761};
CC KM=150 uM for magnesium {ECO:0000269|PubMed:16083926,
CC ECO:0000269|PubMed:9371761};
CC KM=7.0 uM for Manganese {ECO:0000269|PubMed:16083926,
CC ECO:0000269|PubMed:9371761};
CC pH dependence:
CC Optimum pH is 6.75-7.25. {ECO:0000269|PubMed:16083926,
CC ECO:0000269|PubMed:9371761};
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 {ECO:0000250}.
CC -!- MISCELLANEOUS: The protein CAH10289 described in PubMed:16083926 is
CC inactive.
CC -!- MISCELLANEOUS: Manganese improves the fidelity of the reaction and the
CC products consist of 98% (E)-beta-farnesene and 2% (Z)-beta-farnesene.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AF024615; AAB95209.1; -; mRNA.
DR EMBL; AJ786642; CAH10289.1; -; mRNA.
DR AlphaFoldDB; O48935; -.
DR SMR; O48935; -.
DR BioCyc; MetaCyc:MON-14489; -.
DR SABIO-RK; O48935; -.
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..550
FT /note="Beta-farnesene synthase"
FT /id="PRO_0000412249"
FT MOTIF 301..305
FT /note="DDXXD motif"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MUTAGEN 471
FT /note="L->I: No effect."
FT /evidence="ECO:0000269|PubMed:16083926"
FT MUTAGEN 531
FT /note="S->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16083926"
FT CONFLICT 471
FT /note="L -> I (in Ref. 2; CAH10289)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="S -> L (in Ref. 2; CAH10289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 63830 MW; 6B97434E8B8BDF41 CRC64;
MATNGVVISC LREVRPPMTK HAPSMWTDTF SNFSLDDKEQ QKCSETIEAL KQEARGMLMA
ATTPLQQMTL IDTLERLGLS FHFETEIEYK IELINAAEDD GFDLFATALR FRLLRQHQRH
VSCDVFDKFI DKDGKFEESL SNNVEGLLSL YEAAHVGFRE ERILQEAVNF TRHHLEGAEL
DQSPLLIREK VKRALEHPLH RDFPIVYARL FISIYEKDDS RDELLLKLSK VNFKFMQNLY
KEELSQLSRW WNTWNLKSKL PYARDRVVEA YVWGVGYHYE PQYSYVRMGL AKGVLICGIM
DDTYDNYATL NEAQLFTQVL DKWDRDEAER LPEYMKIVYR FILSIYENYE RDAAKLGKSF
AAPYFKETVK QLARAFNEEQ KWVMERQLPS FQDYVKNSEK TSCIYTMFAS IIPGLKSVTQ
ETIDWIKSEP TLATSTAMIG RYWNDTSSQL RESKGGEMLT ALDFHMKEYG LTKEEAASKF
EGLVEETWKD INKEFIATTN YNVGREIAIT FLNYARICEA SYSKTDGDAY SDPNVAKANV
VALFVDAIVF
