KSB_CUCMA
ID KSB_CUCMA Reviewed; 789 AA.
AC Q39548;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ent-kaur-16-ene synthase, chloroplastic;
DE EC=4.2.3.19;
DE AltName: Full=Ent-kaurene synthase;
DE AltName: Full=Ent-kaurene synthase B;
DE Short=KSB;
DE Flags: Precursor;
OS Cucurbita maxima (Pumpkin) (Winter squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Riesenmelone gelb vernetzt; TISSUE=Immature seed;
RX PubMed=8771778; DOI=10.1046/j.1365-313x.1996.10020203.x;
RA Yamaguchi S., Saito T., Abe H., Yamane H., Murofushi N., Kamiya Y.;
RT "Molecular cloning and characterization of a cDNA encoding the gibberellin
RT biosynthetic enzyme ent-kaurene synthase B from pumpkin (Cucurbita maxima
RT L.).";
RL Plant J. 10:203-213(1996).
RN [2]
RP PROTEIN SEQUENCE OF 217-229; 370-389; 395-403; 434-448 AND 615-622, AND
RP CHARACTERIZATION.
RC STRAIN=cv. Riesenmelone gelb vernetzt; TISSUE=Endosperm;
RX PubMed=12228665; DOI=10.1104/pp.109.4.1239;
RA Saito T., Abe H., Yamane H., Sakurai A., Murofushi N., Takio K.,
RA Takahashi N., Kamiya Y.;
RT "Purification and properties of ent-kaurene synthase B from immature seeds
RT of pumpkin.";
RL Plant Physiol. 109:1239-1245(1995).
CC -!- FUNCTION: Catalyzes the conversion of ent-copalyl diphosphate to the
CC gibberellin precursor ent-kaur-16-ene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58553; EC=4.2.3.19;
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=0.35 uM for copalyl diphosphate;
CC pH dependence:
CC Optimum pH is 6.8-7.5.;
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Abundant in most tissues. Present in low amounts in
CC mature cotyledons.
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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; U43904; AAB39482.1; -; mRNA.
DR PIR; T09672; T09672.
DR AlphaFoldDB; Q39548; -.
DR SMR; Q39548; -.
DR PRIDE; Q39548; -.
DR OrthoDB; 318477at2759; -.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000504608; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009899; F:ent-kaurene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Lyase; Magnesium; Metal-binding;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..789
FT /note="Ent-kaur-16-ene synthase, chloroplastic"
FT /id="PRO_0000033626"
FT MOTIF 536..540
FT /note="DDXXD motif"
FT BINDING 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 680
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 688
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 789 AA; 89362 MW; 8CC87F2884CCD7F2 CRC64;
MYLSRPTGVA RFAASSSSSS SASLFPGVDV DTTTKTGALH FEETKERIKK LFDKVELSVS
AYDTAWVAMV PSPNSLNQPL FPECINWVLD SQHADGSWGL LHNDQLLMKA NLLSTLACVL
TLKRWNIGHD HMSKALDFIK SNIASATDEN QRSPVGFDII FPGMIEYAKD LNLNLPLAPT
NVDALVRKKE LELRSCRSNS EGGKAYLAYV SEGIGKLQDW DMVMQYQRKN GSLFNSPSTT
AAAFMHRNDD GCFDYLRSLL QKFDGSVPTI YPLDIYARLH MVDSLQKFGI ARHFKEEIRS
VLDETYRCWM QGEENIFLDA STCAMAFRML RVEGYDVSSD QLTQFSEDIF PNCLGGYLKD
FGASLELYKA SQIITHPDES VLENINSWTS RFLKHGLSSD SVWSDRTDSV VKQEAVNALE
FPYNATLERL ISKRAMESYS GDIVRISKSP YACLNFGHQD FLELAVEDFN TLQRIHLKEL
EELQRWVVEN KLDELKFFRL HLGYCYFAAA ATLTDPELHD ARIAWAQNGV LTTVVDDFYD
GGGSEEELDN LIELVEKWDP DGEVGYCSKD VEIVFLALHS TVCEIGRRAL VWQGRSVMRN
VIDGWLALLK VMRKEAEWST NKVVPSMGEY MEQAHVSFAL GPIILPMLFF VGPKLSEEMI
GSCEYQKLYK LMSTAGRLKN DIRSYDRECK EGKLNILSLW MIDGGGNVTK EEAIEAIKGD
FERAIRELLG LVLQENTTIP RACKDLFWKL MSIVNLFYME DDGYTSNRLM NTVKAMFEQP
MDLDALLNK
