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ISPS_POPTM
ID   ISPS_POPTM              Reviewed;         595 AA.
AC   Q7XAS7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Isoprene synthase, chloroplastic;
DE            EC=4.2.3.27;
DE   Flags: Precursor;
GN   Name=ISPS;
OS   Populus tremuloides (Quaking aspen).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15653811; DOI=10.1104/pp.104.054445;
RA   Sharkey T.D., Yeh S., Wiberley A.E., Falbel T.G., Gong D., Fernandez D.E.;
RT   "Evolution of the isoprene biosynthetic pathway in kudzu.";
RL   Plant Physiol. 137:700-712(2005).
CC   -!- FUNCTION: Lyase that catalyzes the formation of isoprene from
CC       dimethylallyl diphosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate = diphosphate + isoprene;
CC         Xref=Rhea:RHEA:13369, ChEBI:CHEBI:33019, ChEBI:CHEBI:35194,
CC         ChEBI:CHEBI:57623; EC=4.2.3.27;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC       the catalytic activity, presumably through binding to Mg(2+).
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY341431; AAQ16588.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7XAS7; -.
DR   SMR; Q7XAS7; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0034009; F:isoprene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
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; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..595
FT                   /note="Isoprene synthase, chloroplastic"
FT                   /id="PRO_0000398181"
FT   MOTIF           345..349
FT                   /note="DDXXD motif"
FT   BINDING         345
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   595 AA;  68446 MW;  A55977EDD7F6BBAA CRC64;
     MATELLCLHR PISLTHKLFR NPLPKVIQAT PLTLKLRCSV STENVSFSET ETETRRSANY
     EPNSWDYDYL LSSDTDESIE VHKDKAKKLE AEVRREINNE KAEFLTLLEL IDNVQRLGLG
     YRFESDIRRA LDRFVSSGGF DGVTKTSLHG TALSFRLLRQ HGFEVSQEAF SGFKDQNGNF
     LENLKEDIKA ILSLYEASFL ALEGENILDE AKVFAISHLK ELSEEKIGKE LAEQVSHALE
     LPLHRRTQRL EAVWSIEAYR KKEDANQVLL ELAILDYNMI QSVYQRDLRE TSRWWRRVGL
     ATKLHFARDR LIESFYWAVG VAFEPQYSDC RNSVAKMFSF VTIIDDIYDV YGTLDELELF
     TDAVERWDVN AINDLPDYMK LCFLALYNTI NEIAYDNLKD KGENILPYLT KAWADLCNAF
     LQEAKWLYNK STPTFDDYFG NAWKSSSGPL QLIFAYFAVV QNIKKEEIEN LQKYHDIISR
     PSHIFRLCND LASASAEIAR GETANSVSCY MRTKGISEEL ATESVMNLID ETWKKMNKEK
     LGGSLFAKPF VETAINLARQ SHCTYHNGDA HTSPDELTRK RVLSVITEPI LPFER
 
 
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