CPS4_ORYSJ
ID CPS4_ORYSJ Reviewed; 767 AA.
AC Q0JF02; Q68CM0; Q7XNG1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Syn-copalyl diphosphate synthase, chloroplastic {ECO:0000303|PubMed:15341631};
DE Short=OsCPSsyn {ECO:0000303|PubMed:15255861};
DE Short=Syn-CPP synthase {ECO:0000303|PubMed:15255861};
DE EC=5.5.1.14 {ECO:0000269|PubMed:15255861, ECO:0000269|PubMed:15341631};
DE AltName: Full=OsCPS4 {ECO:0000303|PubMed:23621683};
DE AltName: Full=OsCyc1 {ECO:0000303|PubMed:15341631};
DE Flags: Precursor;
GN Name=CPS4 {ECO:0000303|PubMed:23621683};
GN Synonyms=CYC1 {ECO:0000303|PubMed:15341631};
GN OrderedLocusNames=Os04g0178300 {ECO:0000312|EMBL:BAS87948.1},
GN LOC_Os04g09900 {ECO:0000305};
GN ORFNames=OSJNBa0096F01.12 {ECO:0000312|EMBL:CAE04103.3};
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP 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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=15255861; DOI=10.1111/j.1365-313x.2004.02137.x;
RA Xu M., Hillwig M.L., Prisic S., Coates R.M., Peters R.J.;
RT "Functional identification of rice syn-copalyl diphosphate synthase and its
RT role in initiating biosynthesis of diterpenoid phytoalexin/allelopathic
RT natural products.";
RL Plant J. 39:309-318(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23621683; DOI=10.1111/ppl.12066;
RA Toyomasu T., Usui M., Sugawara C., Otomo K., Hirose Y., Miyao A.,
RA Hirochika H., Okada K., Shimizu T., Koga J., Hasegawa M., Chuba M.,
RA Kawana Y., Kuroda M., Minami E., Mitsuhashi W., Yamane H.;
RT "Reverse-genetic approach to verify physiological roles of rice
RT phytoalexins: characterization of a knockdown mutant of OsCPS4 phytoalexin
RT biosynthetic gene in rice.";
RL Physiol. Plantarum 150:55-62(2014).
CC -!- FUNCTION: Catalyzes the conversion of geranylgeranyl diphosphate to the
CC phytoalexin precursor syn-copalyl diphosphate (PubMed:15341631,
CC PubMed:15255861, PubMed:23621683). Required for the biosynthesis of
CC momilactones that exude from roots and act as allelochemicals against
CC lowland weeds in paddy soil (PubMed:23621683).
CC {ECO:0000269|PubMed:15255861, ECO:0000269|PubMed:15341631,
CC ECO:0000269|PubMed:23621683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = 9alpha-copalyl
CC diphosphate; Xref=Rhea:RHEA:25524, ChEBI:CHEBI:58622,
CC ChEBI:CHEBI:58756; EC=5.5.1.14;
CC Evidence={ECO:0000269|PubMed:15255861, ECO:0000269|PubMed:15341631};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25525;
CC Evidence={ECO:0000269|PubMed:15255861, ECO:0000269|PubMed:15341631};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0JF02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0JF02-2; Sequence=VSP_037143;
CC Name=3;
CC IsoId=Q0JF02-3; Sequence=VSP_037144;
CC -!- INDUCTION: Induced by UV irradiation (PubMed:15341631,
CC PubMed:15255861). Induced by methyl jasmonate (PubMed:15255861).
CC {ECO:0000269|PubMed:15255861, ECO:0000269|PubMed:15341631}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:23621683). Mutant plants exhibit increased
CC susceptibility to the rice blast fungus Magnaporthe grisea, and reduced
CC capacity to inhibit germination and growth of lowland weeds in paddy
CC soil, possibly due to decreased levels of momilactones and oryzalexin S
CC (PubMed:23621683). {ECO:0000269|PubMed:23621683}.
CC -!- MISCELLANEOUS: 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 {ECO:0000305|PubMed:15255861, ECO:0000305|PubMed:15341631}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE04103.3; Type=Erroneous gene model prediction; Evidence={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; AB066270; BAD42451.1; -; mRNA.
DR EMBL; AL662933; CAE04103.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14085.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS87948.1; -; Genomic_DNA.
DR EMBL; AK100631; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK121319; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015637092.1; XM_015781606.1. [Q0JF02-1]
DR AlphaFoldDB; Q0JF02; -.
DR SMR; Q0JF02; -.
DR STRING; 4530.OS04T0178300-02; -.
DR PaxDb; Q0JF02; -.
DR PRIDE; Q0JF02; -.
DR EnsemblPlants; Os04t0178300-01; Os04t0178300-01; Os04g0178300. [Q0JF02-3]
DR EnsemblPlants; Os04t0178300-02; Os04t0178300-02; Os04g0178300. [Q0JF02-2]
DR EnsemblPlants; Os04t0178300-03; Os04t0178300-03; Os04g0178300. [Q0JF02-1]
DR GeneID; 4335090; -.
DR Gramene; Os04t0178300-01; Os04t0178300-01; Os04g0178300. [Q0JF02-3]
DR Gramene; Os04t0178300-02; Os04t0178300-02; Os04g0178300. [Q0JF02-2]
DR Gramene; Os04t0178300-03; Os04t0178300-03; Os04g0178300. [Q0JF02-1]
DR KEGG; osa:4335090; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR HOGENOM; CLU_003125_3_2_1; -.
DR InParanoid; Q0JF02; -.
DR OrthoDB; 700680at2759; -.
DR BioCyc; MetaCyc:CYC1-MON; -.
DR BRENDA; 5.5.1.14; 4460.
DR PlantReactome; R-OSA-1119308; Momilactone biosynthesis.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q0JF02; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0051498; F:syn-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
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 Gene3D; 1.10.600.10; -; 2.
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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Isomerase; Magnesium; Metal-binding;
KW Plant defense; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..767
FT /note="Syn-copalyl diphosphate synthase, chloroplastic"
FT /id="PRO_0000372328"
FT REGION 45..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 365..368
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 58..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 453
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_037143"
FT VAR_SEQ 45..307
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_037144"
FT CONFLICT 142
FT /note="D -> N (in Ref. 1; BAD42451)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Y -> S (in Ref. 1; BAD42451)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="Missing (in Ref. 1; BAD42451)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="L -> I (in Ref. 6; AK121319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 767 AA; 87217 MW; 436367D7CAE2FF42 CRC64;
MPVFTASFQC VTLFGQPASA ADAQPLLQGQ RPFLHLHARR RRPCGPMLIS KSPPYPASEE
TREWEADGQH EHTDELRETT TTMIDGIRTA LRSIGEGEIS ISAYDTSLVA LLKRLDGGDG
PQFPSTIDWI VQNQLPDGSW GDASFFMMGD RIMSTLACVV ALKSWNIHTD KCERGLLFIQ
ENMWRLAHEE EDWMLVGFEI ALPSLLDMAK DLDLDIPYDE PALKAIYAER ERKLAKIPRD
VLHSMPTTLL HSLEGMVDLD WEKLLKLRCL DGSFHCSPAS TATAFQQTGD QKCFEYLDGI
VKKFNGGVPC IYPLDVYERL WAVDRLTRLG ISRHFTSEIE DCLDYIFRNW TPDGLAHTKN
CPVKDIDDTA MGFRLLRLYG YQVDPCVLKK FEKDGKFFCL HGESNPSSVT PMYNTYRASQ
LKFPGDDGVL GRAEVFCRSF LQDRRGSNRM KDKWAIAKDI PGEVEYAMDY PWKASLPRIE
TRLYLDQYGG SGDVWIGKVL HRMTLFCNDL YLKAAKADFS NFQKECRVEL NGLRRWYLRS
NLEKFGGTDP QTTLMTSYFL ASANIFEANR AAERLGWARV ALLADAVSSH FRRIGGPKNS
TSNLEELISL VPFDDAYSGS LREAWKQWLM AWTAKESSQE SIEGDTAILL VRAIEIFGGR
HVLTGQRPDL WEYSQLEQLT SSICCKLSRR VLAQENGEST EKVEEIDQQV DLEMQELTRR
VLQGCSAINR LTRETFLHVV KSFCYVAYCS PETIDSHIDK VIFQDVI
