FPPS1_ARTSI
ID FPPS1_ARTSI Reviewed; 346 AA.
AC Q7XYS9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Farnesyl diphosphate synthase 1;
DE Includes:
DE RecName: Full=Dimethylallyltranstransferase;
DE EC=2.5.1.1;
DE Includes:
DE RecName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE EC=2.5.1.10;
GN Name=FDS-1;
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, COFACTOR, TISSUE SPECIFICITY, 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: Catalyzes the sequential condensation of isopentenyl
CC pyrophosphate (IPP) with the allylic pyrophosphates, dimethylallyl
CC pyrophosphate (DMAPP), and then with the resultant geranylpyrophosphate
CC (GPP) to the ultimate product farnesyl pyrophosphate (FPP). Has a 4.5
CC time greater affinity for GPP versus DMAPP.
CC {ECO:0000269|PubMed:12782626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12782626};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12782626};
CC Note=Binds Mg(2+) or Mn(2+). Maximal rates of activity with 1 to 4 mM
CC Mg(2+) and only one third of activity with Mn(2+). No activity with
CC Zn(2+) or Ca(2+). {ECO:0000269|PubMed:12782626};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:12782626};
CC KM=1.6 uM for geranyl diphosphate {ECO:0000269|PubMed:12782626};
CC KM=5.5 uM for isopentenyl pyrophosphate
CC {ECO:0000269|PubMed:12782626};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:12782626};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:12782626};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- TISSUE SPECIFICITY: Highly expressed in shoots.
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; AY308477; AAP74720.1; -; mRNA.
DR PDB; 4KK2; X-ray; 2.20 A; A/B=73-346.
DR PDBsum; 4KK2; -.
DR AlphaFoldDB; Q7XYS9; -.
DR SMR; Q7XYS9; -.
DR BRENDA; 2.5.1.10; 8609.
DR SABIO-RK; Q7XYS9; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..346
FT /note="Farnesyl diphosphate synthase 1"
FT /id="PRO_0000405123"
FT MOTIF 97..101
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT MOTIF 236..240
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 52
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 55
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 90
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 106
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 194
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT HELIX 73..100
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4KK2"
FT TURN 116..120
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 121..141
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 147..172
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 219..242
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:4KK2"
FT TURN 254..258
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 303..323
FT /evidence="ECO:0007829|PDB:4KK2"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:4KK2"
SQ SEQUENCE 346 AA; 39694 MW; 1C5B43A83A88AB90 CRC64;
MSSSKSIDLK SKFLKVYDTL KSDLINDPAF EFDDDSRQWI QKMLDYNVPG GKLNRGLSVV
DSYQLLKGGE LSDDEIFLSS ALGWCIEWLQ AYFLVLDDIM DESHTRRGQP CWFRLPKVGM
IAANDGILLR NHVPRILKKH FRGKPYYVDL VDLFNEVEFQ TASGQMIDLI TTLVGEKDLS
KYSLSIHRRI VQYKTAYYSF YLPVACALLM FGEDLDKHVE VKNVLVEMGT YFQVQDDYLD
CFGAPEVIGK IGTDIEDFKC SWLVVKALEL ANEEQKKTLH ENYGKKDPAS VAKVKEVYHT
LNLQAVFEDY EATSYKKLIT SIENHPSKAV QAVLKSFLGK IYKRQK
