FPPS1_ARATH
ID FPPS1_ARATH Reviewed; 384 AA.
AC Q09152; Q42573; Q8W504; Q93Y84;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Farnesyl pyrophosphate synthase 1, mitochondrial;
DE Short=FPP synthase 1;
DE Short=FPS 1;
DE EC=2.5.1.10;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 1;
DE AltName: Full=Dimethylallyltranstransferase 1;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 1;
DE AltName: Full=Geranyltranstransferase 1;
DE Flags: Precursor;
GN Name=FPS1; OrderedLocusNames=At5g47770; ORFNames=MCA23.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE INITIATION.
RC STRAIN=cv. Columbia;
RX PubMed=9182568; DOI=10.1074/jbc.272.24.15381;
RA Cunillera N., Boronat A., Ferrer A.;
RT "The Arabidopsis thaliana FPS1 gene generates a novel mRNA that encodes a
RT mitochondrial farnesyl-diphosphate synthase isoform.";
RL J. Biol. Chem. 272:15381-15388(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-384.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7858223; DOI=10.1007/bf00019499;
RA Delourme D., Lacroute F., Karst F.;
RT "Cloning of an Arabidopsis thaliana cDNA coding for farnesyl diphosphate
RT synthase by functional complementation in yeast.";
RL Plant Mol. Biol. 26:1867-1873(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 42-384.
RC STRAIN=cv. Columbia;
RX PubMed=8631820; DOI=10.1074/jbc.271.13.7774;
RA Cunillera N., Arro M., Delourme D., Karst F., Boronat A., Ferrer A.;
RT "Arabidopsis thaliana contains two differentially expressed farnesyl-
RT diphosphate synthase genes.";
RL J. Biol. Chem. 271:7774-7780(1996).
CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC pyrophosphate with the allylic pyrophosphates, dimethylallyl
CC pyrophosphate, and then with the resultant geranylpyrophosphate to the
CC ultimate product farnesyl pyrophosphate.
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=(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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
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 -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial; Synonyms=FPS1L;
CC IsoId=Q09152-1; Sequence=Displayed;
CC Name=Cytoplasmic; Synonyms=FPS1S;
CC IsoId=Q09152-2; Sequence=VSP_018808;
CC -!- TISSUE SPECIFICITY: The FPS1L mRNA accumulates preferentially in
CC inflorescences, whereas the FPS1S mRNA is predominantly expressed in
CC roots and inflorescences.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; U80605; AAB49290.1; -; mRNA.
DR EMBL; L46367; AAF44787.1; -; Genomic_DNA.
DR EMBL; L46367; AAB07264.1; -; Genomic_DNA.
DR EMBL; AB016886; BAB11324.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95570.1; -; Genomic_DNA.
DR EMBL; AF370324; AAK44139.1; -; mRNA.
DR EMBL; AY063112; AAL34286.1; -; mRNA.
DR EMBL; X75789; CAA53433.1; -; mRNA.
DR PIR; S52009; S52009.
DR RefSeq; NP_199588.1; NM_124151.3. [Q09152-1]
DR AlphaFoldDB; Q09152; -.
DR SMR; Q09152; -.
DR BioGRID; 20076; 2.
DR STRING; 3702.AT5G47770.1; -.
DR iPTMnet; Q09152; -.
DR PaxDb; Q09152; -.
DR PRIDE; Q09152; -.
DR ProteomicsDB; 247377; -. [Q09152-1]
DR EnsemblPlants; AT5G47770.1; AT5G47770.1; AT5G47770. [Q09152-1]
DR GeneID; 834828; -.
DR Gramene; AT5G47770.1; AT5G47770.1; AT5G47770. [Q09152-1]
DR KEGG; ath:AT5G47770; -.
DR Araport; AT5G47770; -.
DR TAIR; locus:2160947; AT5G47770.
DR eggNOG; KOG0711; Eukaryota.
DR HOGENOM; CLU_028376_3_0_1; -.
DR InParanoid; Q09152; -.
DR OMA; HSYQTEI; -.
DR OrthoDB; 1066656at2759; -.
DR PhylomeDB; Q09152; -.
DR BioCyc; ARA:AT5G47770-MON; -.
DR BioCyc; MetaCyc:AT5G47770-MON; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR PRO; PR:Q09152; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q09152; baseline and differential.
DR Genevisible; Q09152; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:TAIR.
DR GO; GO:0004337; F:geranyltranstransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IDA:TAIR.
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 2: Evidence at transcript level;
KW Alternative initiation; Cholesterol biosynthesis; Cholesterol metabolism;
KW Cytoplasm; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Mitochondrion; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..384
FT /note="Farnesyl pyrophosphate synthase 1, mitochondrial"
FT /id="PRO_0000016469"
FT BINDING 89
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 92
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 128
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 144
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 232
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 271
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_018808"
FT CONFLICT 218
FT /note="A -> S (in Ref. 5; CAA53433)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="Y -> H (in Ref. 5; CAA53433)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="P -> T (in Ref. 5; CAA53433)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 44261 MW; E6808489D07D4F29 CRC64;
MSVSCCCRNL GKTIKKAIPS HHLHLRSLGG SLYRRRIQSS SMETDLKSTF LNVYSVLKSD
LLHDPSFEFT NESRLWVDRM LDYNVRGGKL NRGLSVVDSF KLLKQGNDLT EQEVFLSCAL
GWCIEWLQAY FLVLDDIMDN SVTRRGQPCW FRVPQVGMVA INDGILLRNH IHRILKKHFR
DKPYYVDLVD LFNEVELQTA CGQMIDLITT FEGEKDLAKY SLSIHRRIVQ YKTAYYSFYL
PVACALLMAG ENLENHIDVK NVLVDMGIYF QVQDDYLDCF ADPETLGKIG TDIEDFKCSW
LVVKALERCS EEQTKILYEN YGKPDPSNVA KVKDLYKELD LEGVFMEYES KSYEKLTGAI
EGHQSKAIQA VLKSFLAKIY KRQK
