ID   Q8WS25_TRYCR            Unreviewed;       316 AA.
AC   Q8WS25;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   02-SEP-2026, entry version 96.
DE   SubName: Full=Farnesyl diphosphate synthase {ECO:0000313|EMBL:AAL73358.1};
DE   Flags: Fragment;
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693 {ECO:0000313|EMBL:AAL73358.1};
RN   [1] {ECO:0000313|EMBL:AAL73358.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ferella M.A., Bontempi E.J.;
RT   "Sequencing and characterization of a mitochondrial farnesyl diphosphate
RT   synthase of Trypanosoma cruzi.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:3ID0}
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MG(2+).
RX   PubMed=19876942; DOI=10.1002/prot.22614;
RA   Huang C.H., Gabelli S.B., Oldfield E., Amzel L.M.;
RT   "Binding of nitrogen-containing bisphosphonates (N-BPs) to the Trypanosoma
RT   cruzi farnesyl diphosphate synthase homodimer.";
RL   Proteins 78:888-899(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC       {ECO:0000256|RuleBase:RU004466}.
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DR   EMBL; AF386103; AAL73358.1; -; mRNA.
DR   PDB; 3ID0; X-ray; 2.81 A; A=1-316.
DR   AlphaFoldDB; Q8WS25; -.
DR   SMR; Q8WS25; -.
DR   VEuPathDB; TriTrypDB:BCY84_06991; -.
DR   VEuPathDB; TriTrypDB:C3747_22g238; -.
DR   VEuPathDB; TriTrypDB:C4B63_49g65; -.
DR   VEuPathDB; TriTrypDB:ECC02_007468; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_199; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0094470; -.
DR   VEuPathDB; TriTrypDB:TcCL_NonESM00446; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508323.9; -.
DR   VEuPathDB; TriTrypDB:TcCLB.511823.70; -.
DR   VEuPathDB; TriTrypDB:TCDM_09927; -.
DR   VEuPathDB; TriTrypDB:TcG_08390; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_001798; -.
DR   BRENDA; 2.5.1.10; 6524.
DR   EvolutionaryTrace; Q8WS25; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004337; F:(2E,6E)-farnesyl diphosphate synthase activity; IEA:TreeGrafter.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:TreeGrafter.
DR   GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   FunFam; 1.10.600.10:FF:000033; Farnesyl pyrophosphate synthase; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR039702; FPS1-like.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR11525:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 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.
DR   PDBsum; 3ID0; -.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3ID0};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:3ID0};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004466}.
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:3ID0"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAL73358.1"
SQ   SEQUENCE   316 AA;  35735 MW;  890D21A9AE9BE454 CRC64;
     GKYFRGMTVV NVAEGFLAVT QHDEATKERI LHDACVGGWM IEFLQAHYLV EDDIMDGSVM
     RRGKPCWYRF PGVTTQCAIN DGIILKSWTQ IMAWHYFADR PFLKDLLCLF QKVDYATAVG
     QMYDVTSMCD SNKLDPEVAQ PMTTDFAEFT PAIYKRIVKY KTTFYTYLLP LVMGLFVSEA
     AASVEMNLVE RVAHLIGEYF QVQDDVMDCF TPPEQLGKVG TDIEDAKCSW LAVTFLGKAN
     AAQVAEFKAN YGDKDPAKVA VVKRLYSEAN LQADFAAYEA EVVREVESLI EQLKVKSPTF
     AESVAVVWEK THKRKK
//