ID ISPA_ECOLI Reviewed; 299 AA.
AC P22939; Q2MC05;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 27-MAR-2024, entry version 176.
DE RecName: Full=Farnesyl diphosphate synthase;
DE Short=FPP synthase;
DE EC=2.5.1.10;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE AltName: Full=Geranyltranstransferase;
GN Name=ispA; OrderedLocusNames=b0421, JW0411;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2089044; DOI=10.1093/oxfordjournals.jbchem.a123327;
RA Fujisaki S., Hara H., Nishimura Y., Horiuchi K., Nishino T.;
RT "Cloning and nucleotide sequence of the ispA gene responsible for farnesyl
RT diphosphate synthase activity in Escherichia coli.";
RL J. Biochem. 108:995-1000(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH MAGNESIUM;
RP ISOPENTENYL DIPHOSPHATE AND DIMETHYLALLYL S-THIOLODIPHOSPHATE, SUBUNIT, AND
RP COFACTOR.
RX PubMed=14672944; DOI=10.1074/jbc.c300511200;
RA Hosfield D.J., Zhang Y., Dougan D.R., Broun A., Tari L.W., Swanson R.V.,
RA Finn J.;
RT "Structural basis for bisphosphonate-mediated inhibition of isoprenoid
RT biosynthesis.";
RL J. Biol. Chem. 279:8526-8529(2004).
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;
CC Evidence={ECO:0000269|PubMed:14672944};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:14672944};
CC -!- INTERACTION:
CC P22939; P77609: flxA; NbExp=6; IntAct=EBI-553011, EBI-553024;
CC P22939; P33221: purT; NbExp=4; IntAct=EBI-553011, EBI-553029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; D00694; BAA00599.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40177.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73524.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76201.1; -; Genomic_DNA.
DR PIR; JQ0665; JQ0665.
DR RefSeq; NP_414955.1; NC_000913.3.
DR RefSeq; WP_000347217.1; NZ_SSZK01000009.1.
DR PDB; 1RQI; X-ray; 2.42 A; A/B=1-299.
DR PDB; 1RQJ; X-ray; 1.95 A; A/B=1-299.
DR PDBsum; 1RQI; -.
DR PDBsum; 1RQJ; -.
DR AlphaFoldDB; P22939; -.
DR SMR; P22939; -.
DR BioGRID; 4259837; 475.
DR BioGRID; 849453; 3.
DR DIP; DIP-10044N; -.
DR IntAct; P22939; 16.
DR STRING; 511145.b0421; -.
DR BindingDB; P22939; -.
DR ChEMBL; CHEMBL1075078; -.
DR DrugBank; DB02270; Dimethylallyl S-Thiolodiphosphate.
DR DrugBank; DB02508; Isopentyl Pyrophosphate.
DR DrugBank; DB04160; Pyrophosphoric acid.
DR DrugCentral; P22939; -.
DR SWISS-2DPAGE; P22939; -.
DR jPOST; P22939; -.
DR PaxDb; 511145-b0421; -.
DR EnsemblBacteria; AAC73524; AAC73524; b0421.
DR GeneID; 945064; -.
DR KEGG; ecj:JW0411; -.
DR KEGG; eco:b0421; -.
DR PATRIC; fig|1411691.4.peg.1856; -.
DR EchoBASE; EB0503; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_0_1_6; -.
DR InParanoid; P22939; -.
DR OMA; EGMIGGQ; -.
DR OrthoDB; 9805316at2; -.
DR PhylomeDB; P22939; -.
DR BioCyc; EcoCyc:FPPSYN-MONOMER; -.
DR BioCyc; MetaCyc:FPPSYN-MONOMER; -.
DR BRENDA; 2.5.1.10; 2026.
DR SABIO-RK; P22939; -.
DR EvolutionaryTrace; P22939; -.
DR PRO; PR:P22939; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:EcoCyc.
DR GO; GO:0004337; F:geranyltranstransferase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IMP:EcoCyc.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IMP:EcoCyc.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR PANTHER; PTHR43281; FARNESYL DIPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR43281:SF1; FARNESYL DIPHOSPHATE SYNTHASE; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="Farnesyl diphosphate synthase"
FT /id="PRO_0000123982"
FT BINDING 45
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 48
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 77
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 95
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT BINDING 96
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:14672944"
FT BINDING 181
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT BINDING 182
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT BINDING 220
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT BINDING 237
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:1RQJ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 63..84
FT /evidence="ECO:0007829|PDB:1RQJ"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 107..127
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:1RQJ"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:1RQJ"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 199..229
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 256..278
FT /evidence="ECO:0007829|PDB:1RQJ"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:1RQJ"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:1RQJ"
SQ SEQUENCE 299 AA; 32160 MW; 15BADD5E135060CA CRC64;
MDFPQQLEAC VKQANQALSR FIAPLPFQNT PVVETMQYGA LLGGKRLRPF LVYATGHMFG
VSTNTLDAPA AAVECIHAYS LIHDDLPAMD DDDLRRGLPT CHVKFGEANA ILAGDALQTL
AFSILSDADM PEVSDRDRIS MISELASASG IAGMCGGQAL DLDAEGKHVP LDALERIHRH
KTGALIRAAV RLGALSAGDK GRRALPVLDK YAESIGLAFQ VQDDILDVVG DTATLGKRQG
ADQQLGKSTY PALLGLEQAR KKARDLIDDA RQSLKQLAEQ SLDTSALEAL ADYIIQRNK
//
