CPSKS_PHASA
ID CPSKS_PHASA Reviewed; 946 AA.
AC O13284;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ent-kaur-16-ene synthase;
DE EC=4.2.3.19;
DE EC=5.5.1.13;
DE AltName: Full=CPS/KS;
DE AltName: Full=Ent-copalyl diphosphate synthase;
DE AltName: Full=Ent-kaurene synthase;
DE AltName: Full=FCPS/KS;
OS Phaeosphaeria sp. (strain L487).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Phaeosphaeria; unclassified Phaeosphaeria.
OX NCBI_TaxID=65784;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9268298; DOI=10.1074/jbc.272.35.21706;
RA Kawaide H., Imai R., Sassa T., Kamiya Y.;
RT "Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA
RT isolation, characterization, and bacterial expression of a bifunctional
RT diterpene cyclase in fungal gibberellin biosynthesis.";
RL J. Biol. Chem. 272:21706-21712(1997).
CC -!- FUNCTION: Catalyzes the conversion of geranylgeranyl diphosphate to the
CC gibberellin precursor ent-kaurene diphosphate in a two step process.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl
CC diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553,
CC ChEBI:CHEBI:58756; EC=5.5.1.13;
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 -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
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}.
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DR EMBL; AB003395; BAA22426.1; -; mRNA.
DR PIR; T00024; T00024.
DR AlphaFoldDB; O13284; -.
DR SMR; O13284; -.
DR KEGG; ag:BAA22426; -.
DR BioCyc; MetaCyc:MON-15993; -.
DR BRENDA; 4.2.3.19; 4709.
DR BRENDA; 5.5.1.13; 4709.
DR UniPathway; UPA00390; -.
DR GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009899; F:ent-kaurene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR017057; Ent-kaurene_synthase_fun.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PIRSF; PIRSF036498; Ent-kaurene_synthase_fungi; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
PE 2: Evidence at transcript level;
KW Isomerase; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..946
FT /note="Ent-kaur-16-ene synthase"
FT /id="PRO_0000186445"
FT MOTIF 656..660
FT /note="DDXXD motif; degenerate"
FT BINDING 656
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 839
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 843
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 847
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 946 AA; 105724 MW; DCC31F00897E4D6B CRC64;
MFAKFDMLEE EARALVRKVG NAVDPIYGFS TTSCQIYDTA WAAMISKEEH GDKVWLFPES
FKYLLEKQGE DGSWERHPRS KTVGVLNTAA ACLALLRHVK NPLQLQDIAA QDIELRIQRG
LRSLEEQLIA WDDVLDTNHI GVEMIVPALL DYLQAEDENV DFEFESHSLL MQMYKEKMAR
FSPESLYRAR PSSALHNLEA LIGKLDFDKV GHHLYNGSMM ASPSSTAAFL MHASPWSHEA
EAYLRHVFEA GTGKGSGGFP GTYPTTYFEL NWVLSTLMKS GFTLSDLECD ELSSIANTIA
EGFECDHGVI GFAPRAVDVD DTAKGLLTLT LLGMDEGVSP APMIAMFEAK DHFLTFLGER
DPSFTSNCHV LLSLLHRTDL LQYLPQIRKT TTFLCEAWWA CDGQIKDKWH LSHLYPTMLM
VQAFAEILLK SAEGEPLHDA FDAATLSRVS ICVFQACLRT LLAQSQDGSW HGQPEASCYA
VLTLAESGRL VLLQALQPQI AAAMEKAADV MQAGRWSCSD HDCDWTSKTA YRVDLVAAAY
RLAAMKASSN LTFTVDDNVS KRSNGFQQLV GRTDLFSGVP AWELQASFLE SALFVPLLRN
HRLDVFDRDD IKVSKDHYLD MIPFTWVGCN NRSRTYVSTS FLFDMMIISM LGYQIDEFFE
AEAAPAFAQC IGQLHQVVDK VVDEVIDEVV DKVVGKVVGK VVGKVVDERV DSPTHEAIAI
CNIEASLRRF VDHVLHHQHV LHASQQEQDI LWRELRAFLH AHVVQMADNS TLAPPGRTFF
DWVRTTAADH VACAYSFAFA CCITSATIGQ GQSMFATVNE LYLVQAAARH MTTMCRMCND
IGSVDRDFIE ANINSVHFPE FSTLSLVADK KKALARLAAY EKSCLTHTLD QFENEVLQSP
RVSSAASGDF RTRKVAVVRF FADVTDFYDQ LYILRDLSSS LKHVGT
