ID   ISPA_BUCAI              Reviewed;         282 AA.
AC   P57537;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=BU465;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13162.1; -; Genomic_DNA.
DR   RefSeq; NP_240276.1; NC_002528.1.
DR   RefSeq; WP_009874417.1; NC_002528.1.
DR   AlphaFoldDB; P57537; -.
DR   SMR; P57537; -.
DR   STRING; 107806.10039128; -.
DR   EnsemblBacteria; BAB13162; BAB13162; BAB13162.
DR   KEGG; buc:BU465; -.
DR   PATRIC; fig|107806.10.peg.474; -.
DR   eggNOG; COG0142; Bacteria.
DR   HOGENOM; CLU_014015_0_1_6; -.
DR   OMA; CEGQALD; -.
DR   Proteomes; UP000001806; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..282
FT                   /note="Farnesyl diphosphate synthase"
FT                   /id="PRO_0000123988"
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   282 AA;  32332 MW;  228B31A6DBCD6445 CRC64;
     MHFFHLYERY KHRINQKLFY TLNQLPFQKS SLLKAMKYSV FSGSKRLRSS LIYSTGDVFK
     VNITTLDVIS TAIEFIHSYS LIHDDLPCMD NDNFRRGKIS CHVKYGESTS LLAGDALQSL
     AFNILSNSFM PNVSNLKRIK MISELSYSIG SSGMCMGQNL DLEAEKKDVN LSELEIINLY
     KTSFLMRSAV RLVYFSSNNF SKSILSILDL FSISIGLAFQ IQDDILDFKK DSVKTDNKKI
     IKKHTYPLII GLDESRKKIK QLHKKSFLAL NSLKKKISIP TY