LABER_LAVAN
ID LABER_LAVAN Reviewed; 538 AA.
AC Q2XSC4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Exo-alpha-bergamotene synthase;
DE Short=LaBERS;
DE EC=4.2.3.81;
DE AltName: Full=Trans-alpha-bergamotene synthase;
OS Lavandula angustifolia (Lavender).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Lavandulinae;
OC Lavandula.
OX NCBI_TaxID=39329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17662687; DOI=10.1016/j.abb.2007.06.011;
RA Landmann C., Fink B., Festner M., Dregus M., Engel K.H., Schwab W.;
RT "Cloning and functional characterization of three terpene synthases from
RT lavender (Lavandula angustifolia).";
RL Arch. Biochem. Biophys. 465:417-429(2007).
CC -!- FUNCTION: Catalyzes a mixture of sesquiterpenoids from (2E,6E)-farnesyl
CC diphosphate. Catalyzes the formation of exo-alpha-bergamotene, as well
CC as (E)-nerolidol, (Z)-alpha-bisabolene, (E)-beta-farnesene and beta-
CC sesquiphellandrene. Also has activity towards geranyl diphosphate, but
CC to a much lesser extent. {ECO:0000269|PubMed:17662687}.
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:17662687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.7 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:17662687};
CC KM=3.3 uM for geranyl diphosphate {ECO:0000269|PubMed:17662687};
CC Note=kcat is 0.033 sec(-1) with (2E,6E)-farnesyl diphosphate as
CC substrate. kcat is 0.00026 sec(-1) with geranyl diphosphate as
CC substrate.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17662687};
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; DQ263742; ABB73046.1; -; mRNA.
DR AlphaFoldDB; Q2XSC4; -.
DR SMR; Q2XSC4; -.
DR KEGG; ag:ABB73046; -.
DR BioCyc; MetaCyc:MON-14818; -.
DR BRENDA; 4.2.3.81; 9723.
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 GO; GO:0046246; P:terpene biosynthetic process; IEA:UniProt.
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 Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..538
FT /note="Exo-alpha-bergamotene synthase"
FT /id="PRO_0000418949"
FT MOTIF 291..295
FT /note="DDXXD motif"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 538 AA; 62405 MW; E21A362A94398B89 CRC64;
MEARRSGNFE SSIWDDDYIQ SLTSSYTGKM YVDKSEKLKI EVKMMMDEAT DELEQLELIN
DLQRLGISYH FKDGIAKMLN NIYKSDSKYM EKDLHLTALK FRLLRQHGYR VPQDVFSSFM
DDEGNFEAWV VEDVSVLVSL YEASHISVEG ESILDMAKDF SSHHLTEMVE QIGEACLAEQ
VKRTLELPLH WRVGRLEARW FVQAYETRPN SNPTLVELAK LDFNMVQAKY QDELKRCSRW
YEETGLPEKM SFARHRLAEC FLWSLGFIPD PHHGYSREIM TKIAVLITIT DDIYDIYGAL
EELQEFTEAF ERWDINSLDL LPEYMQICFL AIFNSANELG YQILRDQGLN IIPNLKRSWA
ELSRAYYLEA RWFHNGFVPT TDQYLNTAWI SISGPLLLSY GYLTTTNPIN NKELKSLEKH
PSIIRWPSMV LRLADDLGTS SEEIKRGDVS KSIQCYMNET GCCEGDARHH VKSLIEVALK
RMNDEILMEK PFKSFDTNAM NLARISLCFY QYGDGFGKPH SDTIKNLVSL IVLPFHMP
