ID   ISPA_AQUAE              Reviewed;         262 AA.
AC   O66952;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=aq_748;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC06913.1; -; Genomic_DNA.
DR   PIR; E70365; E70365.
DR   RefSeq; NP_213513.1; NC_000918.1.
DR   RefSeq; WP_010880451.1; NC_000918.1.
DR   AlphaFoldDB; O66952; -.
DR   SMR; O66952; -.
DR   STRING; 224324.aq_748; -.
DR   EnsemblBacteria; AAC06913; AAC06913; aq_748.
DR   KEGG; aae:aq_748; -.
DR   PATRIC; fig|224324.8.peg.596; -.
DR   eggNOG; COG0142; Bacteria.
DR   HOGENOM; CLU_014015_0_1_0; -.
DR   InParanoid; O66952; -.
DR   OMA; HCASLVH; -.
DR   OrthoDB; 1861068at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..262
FT                   /note="Farnesyl diphosphate synthase"
FT                   /id="PRO_0000123984"
FT   BINDING         40
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         43
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         72
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         90
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         171
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  30037 MW;  400592121D46C25E CRC64;
     MERIETWKEK IEKRLNEILK PEGPEELIEA MKYYPLQKGK RIRPLFTVAV ASALGGNEDD
     AITVGSGIEL IHNYSLIHDD LPCMDNDVWR RGLPTCHIKF GEAMALLAGD ALLTYTFEVL
     SQRENYKTLS CEEILEINKI IAQKAGSNGM VGGQVLDIKG YEDLYEVSVK KTGALFEACF
     MCGAVVAKRR EKLKEMESIG RKVGLLFQMV DDYLDKDGFY EKLGECLKEE IKKLYEELKE
     KEIFKESQEL RYLLDLIYKR IT