ID   ISPA_MICLU              Reviewed;         291 AA.
AC   O66126;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=fps;
OS   Micrococcus luteus (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=1270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B-P 26;
RX   PubMed=9515931; DOI=10.1128/jb.180.6.1578-1581.1998;
RA   Shimizu N., Koyama T., Ogura K.;
RT   "Molecular cloning, expression, and characterization of the genes encoding
RT   the two essential protein components of Micrococcus luteus B-P 26
RT   hexaprenyl diphosphate synthase.";
RL   J. Bacteriol. 180:1578-1581(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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AB003187; BAA25265.1; -; Genomic_DNA.
DR   AlphaFoldDB; O66126; -.
DR   SMR; O66126; -.
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..291
FT                   /note="Farnesyl diphosphate synthase"
FT                   /id="PRO_0000123991"
FT   BINDING         44
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         47
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         76
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         94
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         177
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="(2E)-geranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58057"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  32362 MW;  797125AB71E5674A CRC64;
     MLQEKLTMNR DFLNLINESL LNKYHPAQSR LHEAINYSLS AGGKRIRPLL VLTTLDSLGG
     NAHDGLPFGI ALEMIHTYSL IHDDLPAMDN DDYRRGKLTN HKRFDEATAI LAGDALLTDA
     FQCILNTQLN AEIKLSLINL LSTASGSNGM VYGQMLDMQG EHKTLTLNEL ERIHIHKTGE
     LIRAAIVSAG IIMNFNDAQI EQLNIIGKNV GLMFQIKDDI LDVEGSFENI GKTVGSDLNN
     DKSTYVSLLG LEASKQLLND KLTETYDALK TLQPINDNLK TLITYIVERN K