ID   ISPA_BUCAP              Reviewed;         294 AA.
AC   Q8K9A0;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=BUsg_449;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67992.1; -; Genomic_DNA.
DR   RefSeq; WP_011053959.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9A0; -.
DR   SMR; Q8K9A0; -.
DR   STRING; 198804.BUsg_449; -.
DR   EnsemblBacteria; AAM67992; AAM67992; BUsg_449.
DR   KEGG; bas:BUsg_449; -.
DR   eggNOG; COG0142; Bacteria.
DR   HOGENOM; CLU_014015_0_1_6; -.
DR   OMA; CEGQALD; -.
DR   OrthoDB; 1861068at2; -.
DR   Proteomes; UP000000416; 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: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; Transferase.
FT   CHAIN           1..294
FT                   /note="Farnesyl diphosphate synthase"
FT                   /id="PRO_0000123989"
FT   BINDING         45
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         48
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         77
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         84
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="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         95
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         181
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  33881 MW;  7D7D901C7213ED0A CRC64;
     MNFSHLYDIY YNRINKKLFE IIQELPFQDS VLFRAMKYST LSGGKRLRAC LIYATGETFQ
     VNIAALDVIS AAVELVHSYS LIHDDLPCID NDYFRRGKIS CHIKYGENFA LLAGDALQGL
     AFNILSNSNM PGVHDSIRLK MIAEFSNAIG YSGMCIGQML DLEKERKKIN ISELEKINLY
     KTAFLIRCSI RLAYFASNNF SKEVLFILDK FSVSIGLAFQ IQDDILDLKN DIKKLESKRN
     KTKNTYPLLI GLKKSKIKIK ELYKEAFFTL EILKKNFNVN ILKLLTQFIM KRFK