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CARS_LAVAN
ID   CARS_LAVAN              Reviewed;         548 AA.
AC   U3LVZ7;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Beta-caryophyllene synthase {ECO:0000303|PubMed:24078339};
DE            Short=LaCARS {ECO:0000303|PubMed:24078339};
DE            EC=4.2.3.57 {ECO:0000269|PubMed:24078339};
DE   AltName: Full=(-)-beta-caryophyllene synthase {ECO:0000305};
GN   Name=CARS {ECO:0000303|PubMed:24078339};
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, AND CATALYTIC ACTIVITY.
RX   PubMed=24078339; DOI=10.1007/s11103-013-0131-3;
RA   Jullien F., Moja S., Bony A., Legrand S., Petit C., Benabdelkader T.,
RA   Poirot K., Fiorucci S., Guitton Y., Nicole F., Baudino S., Magnard J.L.;
RT   "Isolation and functional characterization of a tau-cadinol synthase, a new
RT   sesquiterpene synthase from Lavandula angustifolia.";
RL   Plant Mol. Biol. 84:227-241(2014).
CC   -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC       sesquiterpenes and sesquiterpenoid alcohols (PubMed:24078339). Converts
CC       farnesyl diphosphate (FPP) to beta-caryophyllene (PubMed:24078339). Can
CC       use geranyl diphosphate (GPP) to produce myrcene, limonene and camphene
CC       (PubMed:24078339). {ECO:0000269|PubMed:24078339}.
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:24078339};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC         Evidence={ECO:0000269|PubMed:24078339};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q40577};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {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:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; JX401283; AGL98419.1; -; mRNA.
DR   AlphaFoldDB; U3LVZ7; -.
DR   SMR; U3LVZ7; -.
DR   BRENDA; 4.2.3.57; 9723.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:1901937; P:beta-caryophyllene biosynthetic process; IDA:UniProtKB.
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   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..548
FT                   /note="Beta-caryophyllene synthase"
FT                   /id="PRO_0000452464"
FT   MOTIF           305..309
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:U3LW50"
FT   BINDING         268
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         305
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         309
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         446
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         449
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         457
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   548 AA;  63644 MW;  402662EA323DCBA4 CRC64;
     MAAPISTNNV CSDDARPVTY HPNVWSDYFL RYTSELTEIS VAKKEEHERQ KEAIRNLLLQ
     TRDDSTLKLE LVDAIQRLGI GYHFEEEIHN SLRNIYDTNP IYNAEDDNLR VAALRFRLIR
     QQGFPAPCDV FRKFVDEEGE FKSWVSNDVE GLLNLYEASN FAVHGEEILE KALEFCSLRL
     EFLTQGMTNS LSMRVKEALK IPISKTLTRL GARKFMSMYQ EDESHNETLL NFAKLDFNLV
     QKIHQKELNQ ITRWWKELDF GKNLPFARDR PVECYFWIVG VYFEPRYGIA RTLLTKIIYL
     ASVLDDIYDV YGTLAELTIF TQIIRRWDSD AMDQLPPYMR IYCKALFDVY VEMEEEMGKI
     RKSYAVEYAK KEMKRLAEMY FQEAQWAFSK YKPTMKEYLK VALISSGYMM MTINSLTTIE
     DLITEEEFNW ILSEPRILRA SLTITRLMDD LAGYGTEGKM SAVHYYMAEN GVSEGEAFKE
     VSGIIKSAWK DVNAECVEPR AASTTILRCV VDFTRVIVLL YSDEDAYGNS QTKTKDLIKS
     VLVDPLII
 
 
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