FPPS_BOVIN
ID FPPS_BOVIN Reviewed; 353 AA.
AC Q8WMY2; A6QPZ8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Farnesyl pyrophosphate synthase;
DE Short=FPP synthase;
DE Short=FPS;
DE EC=2.5.1.10;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE AltName: Full=Dimethylallyltranstransferase;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase;
DE AltName: Full=Geranyltranstransferase;
GN Name=FDPS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BLV G4.
RX PubMed=11773414; DOI=10.1128/jvi.76.3.1400-1414.2002;
RA Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H., Dangoisse O.,
RA Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A., Kettmann R.,
RA Willems L.;
RT "Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1
RT p13(II) accessory proteins interact with farnesyl pyrophosphate
RT synthetase.";
RL J. Virol. 76:1400-1414(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the
CC formation of farnesyl diphosphate (FPP), a precursor for several
CC classes of essential metabolites including sterols, dolichols,
CC carotenoids, and ubiquinones. FPP also serves as substrate for protein
CC farnesylation and geranylgeranylation. Catalyzes the sequential
CC condensation of isopentenyl pyrophosphate with the allylic
CC pyrophosphates, dimethylallyl pyrophosphate, and then with the
CC resultant geranylpyrophosphate to the ultimate product farnesyl
CC pyrophosphate (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Inactivated by interferon-induced RSAD2. This
CC inactivation may result of disruption of lipid rafts at the plasma
CC membrane, and thus have an antiviral effect since many enveloped
CC viruses need lipid rafts to bud efficiently out of the cell (By
CC similarity). {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 -!- SUBUNIT: Homodimer. Interacts with RSAD2 (By similarity). Interacts
CC with bovine leukemia virus (BLV) protein G4. {ECO:0000250,
CC ECO:0000269|PubMed:11773414}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AF461050; AAL58886.1; -; mRNA.
DR EMBL; BC149572; AAI49573.1; -; mRNA.
DR RefSeq; NP_803463.1; NM_177497.2.
DR RefSeq; XP_005203665.1; XM_005203608.2.
DR AlphaFoldDB; Q8WMY2; -.
DR SMR; Q8WMY2; -.
DR PeptideAtlas; Q8WMY2; -.
DR PRIDE; Q8WMY2; -.
DR Ensembl; ENSBTAT00000009272; ENSBTAP00000009272; ENSBTAG00000003948.
DR GeneID; 281156; -.
DR KEGG; bta:281156; -.
DR CTD; 2224; -.
DR VEuPathDB; HostDB:ENSBTAG00000003948; -.
DR GeneTree; ENSGT00900000141074; -.
DR HOGENOM; CLU_028376_0_1_1; -.
DR InParanoid; Q8WMY2; -.
DR OrthoDB; 1066656at2759; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000003948; Expressed in diaphragm and 106 other tissues.
DR ExpressionAtlas; Q8WMY2; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
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:0006695; P:cholesterol biosynthetic process; 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; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
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 Acetylation; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW Host-virus interaction; Hydroxylation; Isoprene biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..353
FT /note="Farnesyl pyrophosphate synthase"
FT /id="PRO_0000237610"
FT BINDING 57
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 60
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 96
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 112
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 200
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT SITE 98
FT /note="Important for determining product chain length"
FT /evidence="ECO:0000250"
FT SITE 99
FT /note="Important for determining product chain length"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14324"
SQ SEQUENCE 353 AA; 40510 MW; 6FCAA8526E0826BE CRC64;
MNGDQKLDAY AQERQDFIQH FSQIVKVLTE EDIGHPEIGD AITRLKEVLE YNAIGGKYNR
GLTVVITFRE LVEPGKQDPD SLQRALTVGW CVELLQAFFL VSDDIMDSSL TRRGQTCWYQ
KPGIGLDAIN DAFLLESSIY RLLKLYCREQ PYYLDLIELF LQSSYQTEIG QTLDLITAPQ
GNVDLGRFTE KRYKSIVKYK TAFYSFYLPV AAAMYMAGID GEKEHAHAKK ILLEMGEFFQ
IQDDYLDLFG DPSMTGKIGT DIQDNKCSWL VVQCLQRASP EQRQILQENY GQKEAEKVAR
VKALYEEMNL SAVYMQYEED SYNHIMGLIE QYAAPLPPAI FLGLAQKIYK RKK
