CPS1_ORYSJ
ID CPS1_ORYSJ Reviewed; 867 AA.
AC Q6ET36; A0A0P0VHK1; Q68BJ4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ent-copalyl diphosphate synthase 1, chloroplastic;
DE Short=Ent-CDP synthase 1;
DE Short=OsCPS1;
DE Short=OsCPS1ent;
DE EC=5.5.1.13;
DE AltName: Full=Ent-kaurene synthase A;
DE AltName: Full=OsCPS;
DE Flags: Precursor;
GN Name=CPS1; OrderedLocusNames=Os02g0278700, LOC_Os02g17780;
GN ORFNames=P0444A09.11;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-867.
RC STRAIN=cv. Nipponbare;
RX PubMed=15341631; DOI=10.1111/j.1365-313x.2004.02175.x;
RA Ootomo K., Kenmoku H., Oikawa H., Koenig W.A., Toshima H., Mitsuhashi W.,
RA Yamane H., Sassa T., Toyomasu T.;
RT "Biological functions of ent- and syn-copalyl diphosphate synthases in
RT rice: key enzymes for the branch point of gibberellin and phytoalexin
RT biosynthesis.";
RL Plant J. 39:886-893(2004).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=15322373; DOI=10.1271/bbb.68.1814;
RA Fukuda A., Nemoto K., Chono M., Yamaguchi S., Nakajima M., Yamagishi J.,
RA Maekawa M., Yamaguchi I.;
RT "Expression pattern of the copalyl diphosphate synthase gene in developing
RT rice anthers.";
RL Biosci. Biotechnol. Biochem. 68:1814-1816(2004).
RN [6]
RP FUNCTION.
RX PubMed=15542489; DOI=10.1104/pp.104.050567;
RA Prisic S., Xu M., Wilderman P.R., Peters R.J.;
RT "Rice contains two disparate ent-copalyl diphosphate synthases with
RT distinct metabolic functions.";
RL Plant Physiol. 136:4228-4236(2004).
CC -!- FUNCTION: Catalyzes the conversion of geranylgeranyl diphosphate to the
CC gibberellin precursor ent-copalyl diphosphate.
CC {ECO:0000269|PubMed:15542489}.
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:0000305};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing pollen from 7 days before
CC flowering. {ECO:0000269|PubMed:15322373}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity, presumably through binding to Mg(2+).
CC -!- MISCELLANEOUS: 2 different ent-CDP synthases exist in rice, one being
CC involved in gibberellin biosynthesis and the other in phytoalexins
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AP004872; BAD28184.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08464.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS78107.1; -; Genomic_DNA.
DR EMBL; AB126932; BAD42449.2; -; mRNA.
DR RefSeq; XP_015624005.1; XM_015768519.1.
DR AlphaFoldDB; Q6ET36; -.
DR SMR; Q6ET36; -.
DR STRING; 4530.OS02T0278700-01; -.
DR PaxDb; Q6ET36; -.
DR PRIDE; Q6ET36; -.
DR EnsemblPlants; Os02t0278700-01; Os02t0278700-01; Os02g0278700.
DR GeneID; 4329013; -.
DR Gramene; Os02t0278700-01; Os02t0278700-01; Os02g0278700.
DR KEGG; osa:4329013; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR HOGENOM; CLU_003125_3_2_1; -.
DR InParanoid; Q6ET36; -.
DR OMA; KETCLLI; -.
DR OrthoDB; 700680at2759; -.
DR BioCyc; MetaCyc:MON-7941; -.
DR PlantReactome; R-OSA-1119348; Ent-kaurene biosynthesis.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6ET36; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0010333; F:terpene synthase activity; IBA:GO_Central.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR GO; GO:0009685; P:gibberellin metabolic process; IC:Gramene.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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 2: Evidence at transcript level;
KW Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..867
FT /note="Ent-copalyl diphosphate synthase 1, chloroplastic"
FT /id="PRO_0000372325"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 418..421
FT /note="DXDD motif"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
SQ SEQUENCE 867 AA; 98055 MW; 7D86B6D24B50FB31 CRC64;
MIHLHSPPTA PAAFGGAGSA DWRRRRRWSW SSSSRAPVAK GGHLRPCVWR RGGDDGGGED
HHADGGGGGG GGAAWRARAT TAGVSSSSST AKGLQANIIE HETPRITKWP NESRDLDDHQ
QNNEADEEAD DELQPLVEQV RSMLSSMEDG AITASAYDTA WVALVPRLDG EGGTQFPAAV
RWIVGSQLAD GSWGDEALFS AYDRVINTLA CVVALTRWSL HHDQCKQGLQ FLNLNLWRLA
EEEPDTMPIG FEIAFPSLVE AARGLGIDFP YDHPALKGIY ANRELKLKRI PKDMMHIVPT
SILHSLEGMP GLDWQRLLKL QCSDGSFLFS PSATAYALMQ TGDKKCFAYI DRIIKKFDGG
VPNVYPVDLF EHIWVVDRLE RLGISRYFQR EIEQNMDYVN RHWTEDGICW ARNSNVKEVD
DTAMAFRLLR LHGYNVSPSV FKNFEKDGEF FCFVGQSTQA VTGMYNLNRA SQISFPGEDI
LQRARNFSYE FLREREAQGT LHDKWIISKD LPGEVQYTLD FPWYASLPRV EARTYIGQYG
GNDDVWIGKT LYRMPIVNNA TYLELAKQDF NRCQALHQHE LQGLQKWFIE NGLEAFGMTP
EDVLRAYFLA AACIFEPNRA SERLAWARVS VLANTISRHF YSDMSSMKRM ERFMWSSLYE
ENGNVLGLEG YAKDGILART LCQLIDLLSQ ETPPVREGQK CIHNLIRCAW IEWMMQQINM
KDGRYDKGRV MHPGSCTVHN KETCLLIAQI VEICAGRIEE AASMINNTEG SWFIQLASSI
CDSLHAKMLL SQDTKKNETT INQIDKEIEL GMQELAQYLL PRVDDRRINN KTKQTFLSIV
KSCYYAANCS PHMLDQHISE VIFEQVI
