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Database: UniProt
Entry: CHRDS_ARTSI
LinkDB: CHRDS_ARTSI
Original site: CHRDS_ARTSI 
ID   CHRDS_ARTSI             Reviewed;         394 AA.
AC   Q7XYS8;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   22-FEB-2023, entry version 66.
DE   RecName: Full=Monoterpene synthase FDS-5, chloroplastic;
DE   AltName: Full=Chrysanthemyl diphosphate synthase;
DE            Short=CPP synthase;
DE            EC=2.5.1.67;
DE   AltName: Full=Dimethylallyltranstransferase;
DE            EC=2.5.1.1;
DE   AltName: Full=Lavandulyl diphosphate synthase;
DE            Short=LPP synthase;
DE            EC=2.5.1.69;
DE   Flags: Precursor;
GN   Name=FDS-5;
OS   Artemisia spiciformis (Spiked big sagebrush) (Artemisia tridentata
OS   spiciformis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=235357;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=12782626; DOI=10.1074/jbc.m213045200;
RA   Hemmerlin A., Rivera S.B., Erickson H.K., Poulter C.D.;
RT   "Enzymes encoded by the farnesyl diphosphate synthase gene family in the
RT   Big Sagebrush Artemisia tridentata ssp. spiciformis.";
RL   J. Biol. Chem. 278:32132-32140(2003).
RN   [2]
RP   CATALYTIC ACTIVITY.
RX   PubMed=12783539; DOI=10.1021/ja034520g;
RA   Erickson H.K., Poulter C.D.;
RT   "Chrysanthemyl diphosphate synthase. The relationship among chain
RT   elongation, branching, and cyclopropanation reactions in the isoprenoid
RT   biosynthetic pathway.";
RL   J. Am. Chem. Soc. 125:6886-6888(2003).
CC   -!- FUNCTION: Condenses two molecules of dimethylallyl diphosphate (DMAPP)
CC       to produce mainly an irregular monoterpene, chrysanthemyl diphosphate
CC       (CPP) and lower amounts of a branched monoterpene, lavandulyl
CC       diphosphate (LPP). CPP is a precursor of the pyrethrin insecticides.
CC       When incubated with isopentenyl diphosphate (IPP) and DMAPP, catalyzes
CC       three competing isoprenoid condensation reactions, a chain elongation
CC       to give geranyl diphosphate (GPP), a cyclopropanation to give CPP and a
CC       branching to give LPP. {ECO:0000269|PubMed:12782626}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC         geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:128769; EC=2.5.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 dimethylallyl diphosphate = (R,R)-chrysanthemyl diphosphate
CC         + diphosphate; Xref=Rhea:RHEA:14009, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57623, ChEBI:CHEBI:58819; EC=2.5.1.67;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 dimethylallyl diphosphate = (R)-lavandulyl diphosphate +
CC         diphosphate; Xref=Rhea:RHEA:21676, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57623, ChEBI:CHEBI:143949; EC=2.5.1.69;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds Mg(2+) or Mn(2+). {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1430 uM for dimethylallyl diphosphate
CC         {ECO:0000269|PubMed:12782626};
CC         KM=1334 uM for isopentenyl diphosphate {ECO:0000269|PubMed:12782626};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:12782626}.
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}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AY308478; AAP74721.1; -; mRNA.
DR   PDB; 4KK2; X-ray; 2.20 A; A/B=50-120.
DR   PDBsum; 4KK2; -.
DR   AlphaFoldDB; Q7XYS8; -.
DR   SMR; Q7XYS8; -.
DR   KEGG; ag:AAP74721; -.
DR   BRENDA; 2.5.1.1; 8609.
DR   BRENDA; 2.5.1.67; 8609.
DR   BRENDA; 2.5.1.69; 8609.
DR   SABIO-RK; Q7XYS8; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0033849; F:chrysanthemyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033851; F:lavandulyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR039702; FPS1-like.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR11525:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Plastid; Transferase; Transit peptide.
FT   TRANSIT         1..65
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           66..394
FT                   /note="Monoterpene synthase FDS-5, chloroplastic"
FT                   /id="PRO_0000405122"
FT   MOTIF           145..149
FT                   /note="DDXXD motif"
FT   BINDING         100
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         103
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         138
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         154
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         242
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   HELIX           58..72
FT                   /evidence="ECO:0007829|PDB:4KK2"
FT   HELIX           82..95
FT                   /evidence="ECO:0007829|PDB:4KK2"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:4KK2"
FT   HELIX           102..115
FT                   /evidence="ECO:0007829|PDB:4KK2"
SQ   SEQUENCE   394 AA;  45022 MW;  3BB3E9C623BF6AC0 CRC64;
     MASFISLSSK SASWNASSCP HPSVQPFVTR KNVVRYHKPT SSEPSYSPLT TTLSSNLNSQ
     FMQVYETLKS ELIHDPLFEF DDDSRQWVER MIDYTVPGGK MVRGYSVVDS YQLLKGEELT
     EEEAFLACAL GWCTEWFQAF ILLHDDMMDG SHTRRGQPCW FRLPEVGAVA INDGVLLRNH
     VHRILKKHFQ GKAYYVHLVD LFNETEFQTI SGQMIDTISR LAGQKELSKY SMSLNRRIVQ
     YKGAYYSCYL PIACALLMFG ENLDDYVQVK DILVELGMYY QIQNDYLDTF GDPNVFGKTG
     TDIEECKCSW LIAKALELAN EEQKKILSEN YGIKDPAKVA KVKEIYHALN LKGAYEDYET
     NLYENSMKAI KAHPSIAVQA VLKSCLEKMY KGHK
//
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