BCUSY_MAGGA
ID BCUSY_MAGGA Reviewed; 550 AA.
AC B3TPQ6;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Beta-cubebene synthase;
DE Short=Mg25;
DE EC=4.2.3.128;
OS Magnolia grandiflora (Southern magnolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Magnoliaceae;
OC Magnolia.
OX NCBI_TaxID=3406;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND TISSUE SPECIFICITY.
RX PubMed=18467455; DOI=10.1104/pp.108.115824;
RA Lee S., Chappell J.;
RT "Biochemical and genomic characterization of terpene synthases in Magnolia
RT grandiflora.";
RL Plant Physiol. 147:1017-1033(2008).
CC -!- FUNCTION: Sesquiterpene synthase converting farnesyl diphosphate into
CC beta-cubebene (24.5%), alpha-muurolene (19.3%), delta-cadinol (18.6%),
CC delta-elemene (16.0%), tau-muurolene (10.8%), and beta-elemene (10.8%).
CC No activity with geranyl diphosphate or geranylgeranyl diphosphate.
CC {ECO:0000269|PubMed:18467455}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-cubebene + diphosphate;
CC Xref=Rhea:RHEA:32019, ChEBI:CHEBI:10363, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.128;
CC Evidence={ECO:0000269|PubMed:18467455};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:18467455};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000305|PubMed:18467455};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.07 uM for farnesyl diphosphate {ECO:0000269|PubMed:18467455};
CC Note=kcat is 0.35 x 10(-3) sec(-1) for farnesyl diphosphate.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18467455};
CC Temperature dependence:
CC Optimum temperature is 24-26 degrees Celsius.
CC {ECO:0000269|PubMed:18467455};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in young developing leaves and in
CC stamens. Not detected in tepals and carpels.
CC {ECO:0000269|PubMed:18467455}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; EU366429; ACC66281.1; -; Genomic_DNA.
DR AlphaFoldDB; B3TPQ6; -.
DR SMR; B3TPQ6; -.
DR KEGG; ag:ACC66281; -.
DR BioCyc; MetaCyc:MON-14947; -.
DR BRENDA; 4.2.3.128; 13170.
DR SABIO-RK; B3TPQ6; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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; Metal-binding.
FT CHAIN 1..550
FT /note="Beta-cubebene synthase"
FT /id="PRO_0000419800"
FT MOTIF 303..307
FT /note="DDXXD motif"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 63421 MW; BEC626551B7BECF6 CRC64;
MDSPTTQRPN MEIGRAFVNY HPSIWGEHFI AASPDVMRLD AHKGRGEELK EVVRNMFSTV
NDPLLKMNLI DAIQRLGVAY HFEMEIDKAL GQMYDDHING KDDGFDLQTL ALQFRLLRQQ
GYNVSSGVFA KFKDDEGNFS SILSKDTHGL LSLYEAAFLG THGDDILDEA ITFTTVHLKS
TLPHVSAPLT KLVELALEIP LHRRMERLQT RFYISIYEED RERNDVLLEF SKLEFLRLQS
LHQRELRDIS LWWKEMDLLA KLPFTRDRVL EGYFWTVGVY FEPHYSRARM IMTKMIAFAT
VMDDTYDVYG TLEELELLTA TIERWNRGDM DQLPDYMKVI FIALLDGVDA TEDDLTGEGK
SYRIYYLKEA VKDLAKAYLA EARWVSSGYV PTSEEYMKVA LISAVYPMLF VAFLIGMDEV
VTKEVLEWAI HMPTMLRTCS IVARLMDDIP SNKLEQERKH VSSSVECYMK EHGTSYHESI
QKLREMVASG WKDINKECLK PTPVPTAVIN VILNFTRVLE IIYQHRDGYT DASVETKEHI
ASLFVDPIPL
