CPS4_ORYSI
ID CPS4_ORYSI Reviewed; 767 AA.
AC Q6E7D7; A2XQW9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Syn-copalyl diphosphate synthase;
DE Short=OsCPSsyn;
DE Short=Syn-CPP synthase;
DE EC=5.5.1.14;
DE AltName: Full=OsCPS4;
DE AltName: Full=OsCyc1;
GN Name=CPS4; Synonyms=CYC1; ORFNames=OsI_014462;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=cv. IR24;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: Catalyzes the conversion of geranylgeranyl diphosphate to the
CC phytoalexin precursor syn-copalyl diphosphate.
CC {ECO:0000269|PubMed:15255861}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- INDUCTION: By UV irradiation. {ECO:0000269|PubMed:15255861}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity, presumably through binding to Mg(2+).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAY93229.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY530101; AAS98158.1; -; mRNA.
DR EMBL; CM000129; EAY93229.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q6E7D7; -.
DR SMR; Q6E7D7; -.
DR STRING; 39946.Q6E7D7; -.
DR HOGENOM; CLU_003125_3_2_1; -.
DR BRENDA; 5.5.1.14; 4460.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051498; F:syn-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; 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 Isomerase; Magnesium; Metal-binding; Plant defense; Reference proteome.
FT CHAIN 1..767
FT /note="Syn-copalyl diphosphate synthase"
FT /id="PRO_0000372329"
FT REGION 45..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 365..368
FT /note="DXDD motif"
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"
SQ SEQUENCE 767 AA; 87465 MW; C64A200D69EC8E5C CRC64;
MPVFTASFQC VTLFGQPASA ADAQPLLQGQ RPFLHLHARR RRPCGPMLIS KSPPYPASEE
TREWEAEGQH EHTDELRETT TTMIDGIRTA LRSIGEGEIS ISAYDTSLVA LLKRLDGGDG
PQFPSTIDWI VQNQLPDGSW GDASFFMMGD RIMSTLACVV ALKSWNIHTD KCERGLLFIQ
ENMWRLAHEE EDWMLVGFEI ALPSLLDMAK DLDLDIPYDE PALKAIYAER ERKLAKIPRD
VLHAMPTTLL 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
NLERFGGTDP QTTLMTSYFL ASANIFEPNR AAERLGWARV ALLADAVSSH FRRIGGPKNL
TSNLEELISL VPFDDAYSGS LREAWKQWLM AWTAKESSQE SIEGDTAILL VRAIEIFGGR
HVLTGQRPDL WEYSQLEQLT SSICRKLYRR VLAQENGKST EKVEEIDQQL DLEMQELTRR
VLQGCSAINR LTRETFLHVV KSFCYVAYCS PETIDNHIDK VIFQDVI
