ISPS_POPAL
ID ISPS_POPAL Reviewed; 595 AA.
AC Q50L36;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Isoprene synthase, chloroplastic {ECO:0000303|PubMed:15848197};
DE Short=PaIspS {ECO:0000303|PubMed:15848197};
DE EC=4.2.3.27 {ECO:0000269|PubMed:15848197};
DE Flags: Precursor;
GN Name=ISPS {ECO:0000303|PubMed:15848197};
OS Populus alba (White poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION BY LIGHT AND HEAT, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND PATHWAY.
RX PubMed=15848197; DOI=10.1016/j.febslet.2005.03.066;
RA Sasaki K., Ohara K., Yazaki K.;
RT "Gene expression and characterization of isoprene synthase from Populus
RT alba.";
RL FEBS Lett. 579:2514-2518(2005).
CC -!- FUNCTION: Lyase that catalyzes the formation of isoprene from
CC dimethylallyl diphosphate, but not from isopentenyl diphosphate or
CC geranyl diphosphate. {ECO:0000269|PubMed:15848197}.
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 Evidence={ECO:0000269|PubMed:15848197};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13370;
CC Evidence={ECO:0000269|PubMed:15848197};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15848197};
CC Note=Magnesium. Can also use other divalent metal cations, except
CC copper and calcium. {ECO:0000269|PubMed:15848197};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.7 mM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:15848197};
CC pH dependence:
CC Optimum pH is 8.0. Active from pH 6.5 to 9.5.
CC {ECO:0000269|PubMed:15848197};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:15848197};
CC -!- PATHWAY: Terpene metabolism. {ECO:0000269|PubMed:15848197}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15848197}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in leaves.
CC {ECO:0000269|PubMed:15848197}.
CC -!- INDUCTION: Up-regulated by heat stress and continuous light. Down-
CC regulated by continuous dark and cold stress. Not induced by pathogens
CC or treatment with methyl jasmonate or methyl salicylate.
CC {ECO:0000269|PubMed:15848197}.
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 {ECO:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AB198180; BAD98243.1; -; mRNA.
DR AlphaFoldDB; Q50L36; -.
DR SMR; Q50L36; -.
DR KEGG; ag:BAD98243; -.
DR BioCyc; MetaCyc:MON-14888; -.
DR BRENDA; 4.2.3.27; 4969.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0034009; F:isoprene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0071485; P:cellular response to absence of light; IEP:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP:UniProtKB.
DR GO; GO:0050993; P:dimethylallyl diphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0043612; P:isoprene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
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; IPR034741; Terpene_cyclase-like_1_C.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
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_0000398179"
FT MOTIF 345..349
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 595 AA; 68371 MW; B19375046A2C176C CRC64;
MATELLCLHR PISLTHKLFR NPLPKVIQAT PLTLKLRCSV STENVSFTET ETEARRSANY
EPNSWDYDYL LSSDTDESIE VYKDKAKKLE AEVRREINNE KAEFLTLLEL IDNVQRLGLG
YRFESDIRGA LDRFVSSGGF DAVTKTSLHG TALSFRLLRQ HGFEVSQEAF SGFKDQNGNF
LENLKEDIKA ILSLYEASFL ALEGENILDE AKVFAISHLK ELSEEKIGKE LAEQVNHALE
LPLHRRTQRL EAVWSIEAYR KKEDANQVLL ELAILDYNMI QSVYQRDLRE TSRWWRRVGL
ATKLHFARDR LIESFYWAVG VAFEPQYSDC RNSVAKMFSF VTIIDDIYDV YGTLDELELF
TDAVERWDVN AINDLPDYMK LCFLALYNTI NEIAYDNLKD KGENILPYLT KAWADLCNAF
LQEAKWLYNK STPTFDDYFG NAWKSSSGPL QLVFAYFAVV QNIKKEEIEN LQKYHDTISR
PSHIFRLCND LASASAEIAR GETANSVSCY MRTKGISEEL ATESVMNLID ETWKKMNKEK
LGGSLFAKPF VETAINLARQ SHCTYHNGDA HTSPDELTRK RVLSVITEPI LPFER
