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Database: UniProt
Entry: Q3US29_MOUSE
LinkDB: Q3US29_MOUSE
Original site: Q3US29_MOUSE 
ID   Q3US29_MOUSE            Unreviewed;       353 AA.
AC   Q3US29;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000256|ARBA:ARBA00034546};
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000256|ARBA:ARBA00032873};
DE   AltName: Full=Dimethylallyltranstransferase {ECO:0000256|ARBA:ARBA00032448};
DE   AltName: Full=Farnesyl diphosphate synthase {ECO:0000256|ARBA:ARBA00032424};
DE   AltName: Full=Geranyltranstransferase {ECO:0000256|ARBA:ARBA00032380};
GN   Name=Fdps {ECO:0000313|MGI:MGI:104888};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE24508.1};
RN   [1] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE24508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24508.1};
RC   TISSUE=Head {ECO:0000313|EMBL:BAE24508.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
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         Evidence={ECO:0000256|ARBA:ARBA00001744};
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         Evidence={ECO:0000256|ARBA:ARBA00000969};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC       farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC       diphosphate: step 1/1. {ECO:0000256|ARBA:ARBA00005035}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC       geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC       diphosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004932}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC       {ECO:0000256|RuleBase:RU004466}.
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DR   EMBL; AK140881; BAE24508.1; -; mRNA.
DR   AlphaFoldDB; Q3US29; -.
DR   SwissPalm; Q3US29; -.
DR   PeptideAtlas; Q3US29; -.
DR   AGR; MGI:104888; -.
DR   MGI; MGI:104888; Fdps.
DR   ChiTaRS; Fdps; mouse.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
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.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   2: Evidence at transcript level;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Transferase {ECO:0000256|RuleBase:RU004466}.
SQ   SEQUENCE   353 AA;  40509 MW;  9A3F7234AEA9576A CRC64;
     MNGNQKLDAY NQEKQNFIQH FSQIVKVLTE KELGHPEIGD AIARLKEVLE YNALGGKYNR
     GLTVVQAFQE LVEPKKQDAE SLQRALTVGW CVELLQAFFL VSDDIMDSSL TRRGQICWYQ
     KPGIGLDAIN DALLLEASIY RLLKFYCREQ PYYLNLLELF LQSSYQTEIG QTLDLMTAPQ
     GHVDLGRYTE KRYKSIVKYK TAFYSFYLPI AAAMYMAGID GEKEHANALK ILMEMGEFFQ
     VQDDYLDLFG DPSVTGKVGT DIQDNKCSWL VVQCLLRASP QQRQILEENY GQKDPGKVAR
     VKALYEALDL QSAFFKYEED SYNRLKSLIE QCSAPLPPSI FMELANKIYK RRK
//
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