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 03-AUG-2022, entry version 64.
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; -; 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; PTHR11525; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 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
