CASS_RICCO
ID CASS_RICCO Reviewed; 601 AA.
AC P59287; B9RHX1;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Casbene synthase, chloroplastic;
DE EC=4.2.3.8;
DE Flags: Precursor;
GN ORFNames=RCOM_1574350;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8078910; DOI=10.1073/pnas.91.18.8497;
RA Mau C.J., West C.A.;
RT "Cloning of casbene synthase cDNA: evidence for conserved structural
RT features among terpenoid cyclases in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8497-8501(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8954576; DOI=10.1006/abbi.1996.0559;
RA Hill A.M., Cane D.E., Mau C.J., West C.A.;
RT "High level expression of Ricinus communis casbene synthase in Escherichia
RT coli and characterization of the recombinant enzyme.";
RL Arch. Biochem. Biophys. 336:283-289(1996).
CC -!- FUNCTION: Catalyzes the cyclization of geranylgeranyl diphosphate to
CC casbene, a diterpene phytoalexin with antibacterial and antifungal
CC activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = casbene +
CC diphosphate; Xref=Rhea:RHEA:14901, ChEBI:CHEBI:17695,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58756; EC=4.2.3.8;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for geranylgeranyl diphosphate;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: By oligogalacturonide fragments released by fungal
CC infection. Detected after 5 hours of incubation with the pectic
CC fragments and reaches a maximum after 10-12 hours.
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 -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L32134; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EQ973781; EEF48743.1; -; Genomic_DNA.
DR RefSeq; XP_002513340.1; XM_002513294.2.
DR AlphaFoldDB; P59287; -.
DR SMR; P59287; -.
DR STRING; 3988.XP_002513340.1; -.
DR PRIDE; P59287; -.
DR GeneID; 8259981; -.
DR KEGG; rcu:8259981; -.
DR InParanoid; P59287; -.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:MON-14979; -.
DR BRENDA; 4.2.3.8; 1204.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050449; F:casbene 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 GO; GO:0120251; P:hydrocarbon 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 Chloroplast; Lyase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..601
FT /note="Casbene synthase, chloroplastic"
FT /id="PRO_0000033620"
FT MOTIF 355..359
FT /note="DDXXD motif"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 601 AA; 68966 MW; F7B362D286747957 CRC64;
MALPSAAMQS NPEKLNLFHR LSSLPTTSLE YGNNRFPFFS SSAKSHFKKP TQACLSSTTH
QEVRPLAYFP PTVWGNRFAS LTFNPSEFES YDERVIVLKK KVKDILISST SDSVETVILI
DLLCRLGVSY HFENDIEELL SKIFNSQPDL VDEKECDLYT AAIVFRVFRQ HGFKMSSDVF
SKFKDSDGKF KESLRGDAKG MLSLFEASHL SVHGEDILEE AFAFTKDYLQ SSAVELFPNL
KRHITNALEQ PFHSGVPRLE ARKFIDLYEA DIECRNETLL EFAKLDYNRV QLLHQQELCQ
FSKWWKDLNL ASDIPYARDR MAEIFFWAVA MYFEPDYAHT RMIIAKVVLL ISLIDDTIDA
YATMEETHIL AEAVARWDMS CLEKLPDYMK VIYKLLLNTF SEFEKELTAE GKSYSVKYGR
EAFQELVRGY YLEAVWRDEG KIPSFDDYLY NGSMTTGLPL VSTASFMGVQ EITGLNEFQW
LETNPKLSYA SGAFIRLVND LTSHVTEQQR GHVASCIDCY MNQHGVSKDE AVKILQKMAT
DCWKEINEEC MRQSQVSVGH LMRIVNLARL TDVSYKYGDG YTDSQQLKQF VKGLFVDPIS
I
