ISPS_PUEML
ID ISPS_PUEML Reviewed; 608 AA.
AC Q6EJ97;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Isoprene synthase, chloroplastic;
DE EC=4.2.3.27;
DE Flags: Precursor;
GN Name=ISPS;
OS Pueraria montana var. lobata (Kudzu vine) (Pueraria lobata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Pueraria.
OX NCBI_TaxID=3893;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.7 mM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:15653811};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Note=recovered from
CC purified chloroplasts of transgenic Arabidopsis plants.
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 -!- MISCELLANEOUS: Sufficient to confer the trait of isoprene emission when
CC expressed in Arabidopsis.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AY316691; AAQ84170.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6EJ97; -.
DR SMR; Q6EJ97; -.
DR BRENDA; 4.2.3.27; 13960.
DR SABIO-RK; Q6EJ97; -.
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; 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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..608
FT /note="Isoprene synthase, chloroplastic"
FT /id="PRO_0000398182"
FT MOTIF 350..354
FT /note="DDXXD motif"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 608 AA; 70075 MW; 2BE7005A49BB418A CRC64;
MATNLLCLSN KLSSPTPTPS TRFPQSKNFI TQKTSLANPK PWRVICATSS QFTQITEHNS
RRSANYQPNL WNFEFLQSLE NDLKVEKLEE KATKLEEEVR CMINRVDTQP LSLLELIDDV
QRLGLTYKFE KDIIKALENI VLLDENKKNK SDLHATALSF RLLRQHGFEV SQDVFERFKD
KEGGFSGELK GDVQGLLSLY EASYLGFEGE NLLEEARTFS ITHLKNNLKE GINTKVAEQV
SHALELPYHQ RLHRLEARWF LDKYEPKEPH HQLLLELAKL DFNMVQTLHQ KELQDLSRWW
TEMGLASKLD FVRDRLMEVY FWALGMAPDP QFGECRKAVT KMFGLVTIID DVYDVYGTLD
ELQLFTDAVE RWDVNAINTL PDYMKLCFLA LYNTVNDTSY SILKEKGHNN LSYLTKSWRE
LCKAFLQEAK WSNNKIIPAF SKYLENASVS SSGVALLAPS YFSVCQQQED ISDHALRSLT
DFHGLVRSSC VIFRLCNDLA TSAAELERGE TTNSIISYMH ENDGTSEEQA REELRKLIDA
EWKKMNRERV SDSTLLPKAF MEIAVNMARV SHCTYQYGDG LGRPDYATEN RIKLLLIDPF
PINQLMYV
