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CPS2_ORYSI
ID   CPS2_ORYSI              Reviewed;         800 AA.
AC   Q5MQ85;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Ent-copalyl diphosphate synthase 2;
DE            Short=Ent-CDP synthase 2;
DE            Short=OsCPS2;
DE            Short=OsCPS2ent;
DE            EC=5.5.1.13;
DE   AltName: Full=Ent-kaurene synthase A;
DE   AltName: Full=OsCyc2;
GN   Name=CPS2; Synonyms=CYC2; ORFNames=OsI_007598;
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=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).
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 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   -!- INDUCTION: By UV irradiation. {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+).
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}.
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DR   EMBL; AY602991; AAT11021.1; -; mRNA.
DR   EMBL; CM000127; EAY86365.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5MQ85; -.
DR   SMR; Q5MQ85; -.
DR   STRING; 39946.Q5MQ85; -.
DR   EnsemblPlants; BGIOSGA008469-TA; BGIOSGA008469-PA; BGIOSGA008469.
DR   Gramene; BGIOSGA008469-TA; BGIOSGA008469-PA; BGIOSGA008469.
DR   HOGENOM; CLU_003125_3_2_1; -.
DR   OMA; RDKWVIA; -.
DR   BRENDA; 5.5.1.13; 4460.
DR   Proteomes; UP000007015; Chromosome 2.
DR   GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; -; 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   Isomerase; Magnesium; Metal-binding; Plant defense; Reference proteome.
FT   CHAIN           1..800
FT                   /note="Ent-copalyl diphosphate synthase 2"
FT                   /id="PRO_0000372327"
FT   REGION          52..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           374..377
FT                   /note="DXDD motif"
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"
SQ   SEQUENCE   800 AA;  90006 MW;  CB19FE6EEE1AB0BE 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 ERRATGNLRD KWVIANGLPS EVEYALDFPW
     KASLPRVETR VYLEQYGASE DAWIGKGLYR MTLVNNDLYL EAAKADFTNF QRLSRLEWLS
     LKRWYIRNNL QAHGVTEQSV LRAYFLAAAN IFEPNRAAER LGWARTAILA EAIASHLRQY
     SANGAADGMT ERLISGLASH DWDWRESNDS AARSLLYALD ELIDLHAFGN ASDSLREAWK
     QWLMSWTNES QGSTGGDTAL LLVRTIEICS GRHGSAEQSL KNSEDYARLE QIASSMCSKL
     ATKILAQNGG SMDNVEGIDQ EVDVEMKELI QRVYGSSSND VSSVTRQTFL DVVKSFCYVA
     HCSPETIDGH ISKVLFEDVN
 
 
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