ISPS_POPCN
ID ISPS_POPCN Reviewed; 595 AA.
AC Q9AR86;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Isoprene synthase, chloroplastic;
DE EC=4.2.3.27;
DE Flags: Precursor;
GN Name=ISPS;
OS Populus canescens (Grey poplar) (Populus tremula x Populus alba).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=80863;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX PubMed=11506373; DOI=10.1007/s004250100557;
RA Miller B., Oschinski C., Zimmer W.;
RT "First isolation of an isoprene synthase gene from poplar and successful
RT expression of the gene in Escherichia coli.";
RL Planta 213:483-487(2001).
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 Evidence={ECO:0000269|PubMed:11506373};
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; AJ294819; CAC35696.1; -; mRNA.
DR PDB; 3N0F; X-ray; 2.70 A; A/B=53-595.
DR PDB; 3N0G; X-ray; 2.80 A; A/B=53-595.
DR PDBsum; 3N0F; -.
DR PDBsum; 3N0G; -.
DR AlphaFoldDB; Q9AR86; -.
DR SMR; Q9AR86; -.
DR KEGG; ag:CAC35696; -.
DR BRENDA; 4.2.3.27; 4978.
DR EvolutionaryTrace; Q9AR86; -.
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 GO; GO:0120251; P:hydrocarbon biosynthetic process; IEA:UniProt.
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 3D-structure; Chloroplast; Lyase; Magnesium; Metal-binding; Plastid;
KW 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_0000398180"
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"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:3N0F"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:3N0F"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3N0G"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:3N0F"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 267..298
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 328..349
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 377..401
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 406..428
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 435..445
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 448..459
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 465..472
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 476..498
FT /evidence="ECO:0007829|PDB:3N0F"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 506..514
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 518..541
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 548..564
FT /evidence="ECO:0007829|PDB:3N0F"
FT HELIX 574..585
FT /evidence="ECO:0007829|PDB:3N0F"
SQ SEQUENCE 595 AA; 68386 MW; 4A5826BDCA5903F7 CRC64;
MATELLCLHR PISLTHKLFR NPLPKVIQAT PLTLKLRCSV STENVSFTET ETEARRSANY
EPNSWDYDFL LSSDTDESIE VYKDKAKKLE AEVRREINNE KAEFLTLLEL IDNVQRLGLG
YRFESDIRRA LDRFVSSGGF DGVTKTSLHA TALSFRLLRQ HGFEVSQEAF SGFKDQNGNF
LENLKEDTKA ILSLYEASFL ALEGENILDE ARVFAISHLK ELSEEKIGKE LAEQVNHALE
LPLHRRTQRL EAVWSIEAYR KKEDANQVLL ELAILDYNMI QSVYQRDLRE TSRWWRRVGL
ATKLHFAKDR LIESFYWAVG VAFEPQYSDC RNSVAKMFSF VTIIDDIYDV YGTLDELELF
TDAVERWDVN AINDLPDYMK LCFLALYNTI NEIAYDNLKD KGENILPYLT KAWADLCNAF
LQEAKWLYNK STPTFDDYFG NAWKSSSGPL QLIFAYFAVV QNIKKEEIEN LQKYHDIISR
PSHIFRLCND LASASAEIAR GETANSVSCY MRTKGISEEL ATESVMNLID ETCKKMNKEK
LGGSLFAKPF VETAINLARQ SHCTYHNGDA HTSPDELTRK RVLSVITEPI LPFER
