CPS2_ORYSJ
ID CPS2_ORYSJ Reviewed; 800 AA.
AC Q6Z5I0; Q0E085; Q68CL9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ent-copalyl diphosphate synthase 2, chloroplastic {ECO:0000303|PubMed:15542489};
DE Short=Ent-CDP synthase 2 {ECO:0000303|PubMed:15542489};
DE Short=OsCPS2 {ECO:0000303|PubMed:15542489};
DE Short=OsCPS2ent {ECO:0000303|PubMed:15542489};
DE EC=5.5.1.13 {ECO:0000269|PubMed:15542489};
DE AltName: Full=Diterpene cyclase 2 {ECO:0000303|PubMed:15341631};
DE Short=OsCyc2 {ECO:0000303|PubMed:15341631};
DE AltName: Full=Ent-kaurene synthase A;
DE Flags: Precursor;
GN Name=CPS2 {ECO:0000303|PubMed:15542489};
GN Synonyms=CYC2 {ECO:0000303|PubMed:15341631};
GN OrderedLocusNames=Os02g0571100 {ECO:0000305}, LOC_Os02g36210 {ECO:0000305};
GN ORFNames=OsJ_006996 {ECO:0000312|EMBL:EAZ23513.1},
GN P0689H05.16 {ECO:0000312|EMBL:BAD17267.1};
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 [MRNA], AND INDUCTION.
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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION, INDUCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Nipponbare;
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 phytoalexin 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 Evidence={ECO:0000269|PubMed:15542489};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
CC Evidence={ECO:0000269|PubMed:15542489};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:15542489}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: By UV irradiation. {ECO:0000269|PubMed:15341631,
CC ECO:0000269|PubMed:15542489}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity, presumably through binding to Mg(2+). {ECO:0000305}.
CC -!- MISCELLANEOUS: 2 different ent-CDP synthases exist in rice, one being
CC involved in gibberellin biosynthesis and the other in phytoalexins
CC biosynthesis. Phytoalexins are diterpenoid secondary metabolites
CC involved in the defense mechanism of the plant and produced in response
CC to attack (by a pathogen, elicitor or UV irradiation).
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD42452.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAF09103.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB066271; BAD42452.1; ALT_FRAME; mRNA.
DR EMBL; AP005114; BAD17267.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09103.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000139; EAZ23513.1; -; Genomic_DNA.
DR RefSeq; XP_015625954.1; XM_015770468.1.
DR AlphaFoldDB; Q6Z5I0; -.
DR SMR; Q6Z5I0; -.
DR STRING; 4530.OS02T0571100-01; -.
DR PaxDb; Q6Z5I0; -.
DR PRIDE; Q6Z5I0; -.
DR EnsemblPlants; Os02t0571100-01; Os02t0571100-01; Os02g0571100.
DR GeneID; 9266189; -.
DR Gramene; Os02t0571100-01; Os02t0571100-01; Os02g0571100.
DR KEGG; osa:9266189; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR HOGENOM; CLU_003125_3_3_1; -.
DR InParanoid; Q6Z5I0; -.
DR OrthoDB; 372122at2759; -.
DR BioCyc; MetaCyc:CYC2-MON; -.
DR BRENDA; 5.5.1.13; 4460.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6Z5I0; baseline and differential.
DR Genevisible; Q6Z5I0; 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:0006952; P:defense response; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Chloroplast; Isomerase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..800
FT /note="Ent-copalyl diphosphate synthase 2, chloroplastic"
FT /id="PRO_0000372326"
FT REGION 52..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 374..377
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 52..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT CONFLICT 73
FT /note="G -> D (in Ref. 1; BAD42452)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="G -> D (in Ref. 1; BAD42452)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="D -> N (in Ref. 1; BAD42452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 800 AA; 89937 MW; C42E5E5CEA19058D CRC64;
MQMQVLTAAS SLPRATLLRP AAAEPWRQSF LQLQARPIQR PGIMLHCKAQ LQGQETRERR
QLDDDEHARP PQGGDDDVAA STSELPYMIE SIKSKLRAAR NSLGETTVSA YDTAWIALVN
RLDGGGERSP QFPEAIDWIA RNQLPDGSWG DAGMFIVQDR LINTLGCVVA LATWGVHEEQ
RARGLAYIQD NLWRLGEDDE EWMMVGFEIT FPVLLEKAKN LGLDINYDDP ALQDIYAKRQ
LKLAKIPREA LHARPTTLLH SLEGMENLDW ERLLQFKCPA GSLHSSPAAS AYALSETGDK
ELLEYLETAI NNFDGGAPCT YPVDNFDRLW SVDRLRRLGI SRYFTSEIEE YLEYAYRHLS
PDGMSYGGLC PVKDIDDTAM AFRLLRLHGY NVSSSVFNHF EKDGEYFCFA GQSSQSLTAM
YNSYRASQIV FPGDDDGLEQ LRAYCRAFLE ERRATGNLMD KWVIANGLPS EVEYALDFPW
KASLPRVETR VYLEQYGASE DAWIGKGLYR MTLVNNDLYL EAAKADFTNF QRLSRLEWLS
LKRWYIRNNL QAHGVTEQSV LRAYFLAAAN IFEPNRAAER LGWARTAILA EAIASHLRQY
SANGAADGMT ERLISGLASH DWDWRESKDS AARSLLYALD ELIDLHAFGN ASDSLREAWK
QWLMSWTNES QGSTGGDTAL LLVRTIEICS GRHGSAEQSL KNSADYARLE QIASSMCSKL
ATKILAQNGG SMDNVEGIDQ EVDVEMKELI QRVYGSSSND VSSVTRQTFL DVVKSFCYVA
HCSPETIDGH ISKVLFEDVN
