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CPS3_ISOER
ID   CPS3_ISOER              Reviewed;         766 AA.
AC   A0A3G1QTU5;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 2.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Ent-copalyl diphosphate synthase 3 {ECO:0000303|PubMed:30496917};
DE            Short=IeCPS3 {ECO:0000303|PubMed:30496917};
DE            EC=5.5.1.13 {ECO:0000269|PubMed:30496917};
DE   Flags: Precursor; Fragment;
GN   Name=CPS3 {ECO:0000303|PubMed:30496917};
OS   Isodon eriocalyx (Plectranthus eriocalyx).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Isodoninae;
OC   Isodon.
OX   NCBI_TaxID=662907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=30496917; DOI=10.1016/j.phytochem.2018.11.015;
RA   Du G., Gong H.-Y., Feng K.-N., Chen Q.-Q., Yang Y.-L., Fu X.-L., Lu S.,
RA   Zeng Y.;
RT   "Diterpene synthases facilitating production of the kaurane skeleton of
RT   eriocalyxin B in the medicinal plant Isodon eriocalyx.";
RL   Phytochemistry 158:96-102(2019).
CC   -!- FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids
CC       natural products such as oridonin, miltiradiene, eriocalyxin B and
CC       nezukol, known to exhibit antitumor, anti-inflammatory and
CC       antibacterial activities, and in the production of gibberellins
CC       phytohormones (PubMed:30496917). Catalyzes the conversion of
CC       (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl
CC       diphosphate (ent-CPP) (PubMed:30496917). {ECO:0000269|PubMed:30496917}.
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:30496917};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
CC         Evidence={ECO:0000269|PubMed:30496917};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q40577};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC       {ECO:0000305|PubMed:30496917}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:30496917}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Accumulates in leaves, and, at low levels, in
CC       germinating seeds. {ECO:0000269|PubMed:30496917}.
CC   -!- DEVELOPMENTAL STAGE: Moslty expressed in leaves where ent-kaurane
CC       diterpenoids accumulates but weakly expressed in germinating seeds in
CC       which gibberellins are produced. {ECO:0000269|PubMed:30496917}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily.
CC       {ECO:0000305}.
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DR   EMBL; KY937955; AWN06649.1; -; mRNA.
DR   AlphaFoldDB; A0A3G1QTU5; -.
DR   SMR; A0A3G1QTU5; -.
DR   UniPathway; UPA00213; -.
DR   UniPathway; UPA00390; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:1901946; P:miltiradiene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
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; Plastid; Transit peptide.
FT   TRANSIT         <1..30
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..766
FT                   /note="Ent-copalyl diphosphate synthase 3"
FT                   /id="PRO_0000452380"
FT   MOTIF           354..357
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000250|UniProtKB:G3E4M4"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         440
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   766 AA;  87546 MW;  50232FABE369FE77 CRC64;
     FRSTAAGRCL PVTCCVFPRH FRVSSSSILP SNAKVVGGCK KNRQIAVEAA QSLEVDSQQP
     MNQEEVSEKM RQLREKIRWM LQNMDDGEIS VSPYDTAWVA MVEDIGGGGG PQFPTSLEWI
     SNNQLDDGSW GDLRFLIYDR ILNTLACVAV LTQWKMHLHK CQKGLRFIRE NIDNLENGND
     EMMPVGFEVA FPSLIQTAKK VGIKIPTDSP FMKNIYAKRD LKLRKIPMDI LHTKPTTLLH
     SLEGMEGLDW EKLLNLRTDD GSFLMSPSST AYVFRHTKDE LCHQYLLKSV NKFNGGVPNV
     YPVDMFEHLW CVDRLQRLGI SRYFQVEIQE CLDYVYKYWT NKGICWARNT NVQDVDDTAM
     GFRLLRLHGY DVSTDAFKQF EKAGEFCSFP GQSTDALTGM YNLYRASQTM FNGEHILADA
     KEYSTNFLHK KRLANAIVDK WIITKDLPGE VGYALDVPFY ASLPRLEARF FLEQYGGDDD
     VWIGKTLYRM LYVNCDTHLE LAKLDYEKCQ AVHQLEWESI QKWYRDWNLV EFGLSERSLL
     LAYYIAASTV FEPERSRERL AWAITAILVK TIASQRQLPL ETKGESLGSI LENEDGGRLI
     EFLINTIHQL SSEIVVAEGR DITQQLSNTW QKWLKTCKEG GDDDLGEAEA RLIVHTLHLS
     SGLDESSFSH PKYHQLLEAT SKVCGQLRLF QSRKQVDVDL ATGTTFQIEA GMQELVKLVF
     TNSSEDLDSL TKQSFFSIAR SFYYTAYCDE GAINSHIDKV LFEKID
 
 
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