ID FPPS_CHICK Reviewed; 367 AA. AC P08836; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 02-SEP-2026, entry version 131. DE RecName: Full=Farnesyl pyrophosphate synthase; DE Short=FPP synthase; DE Short=FPS; DE EC=2.5.1.10; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase; DE AltName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1; DE AltName: Full=Farnesyl diphosphate synthase; DE AltName: Full=Geranyltranstransferase; GN Name=FDPS; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP PROTEIN SEQUENCE OF 187-216. RC TISSUE=Liver; RX PubMed=7272273; DOI=10.1021/bi00516a007; RA Brems D.N., Bruenger E., Rillings H.C.; RT "Isolation and characterization of a photoaffinity-labeled peptide from the RT catalytic site of prenyltransferase."; RL Biochemistry 20:3711-3718(1981). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-367, SUBUNIT, AND COFACTOR. RC TISSUE=Liver; RX PubMed=8086404; DOI=10.1021/bi00202a004; RA Tarshis L.C., Yan M., Poulter C.D., Sacchettini J.C.; RT "Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A RT resolution."; RL Biochemistry 33:10871-10877(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-367 IN COMPLEXES WITH MAGNESIUM RP IONS; DIMETHYLALLYL DIPHOSPHATE; GERANYL DIPHOSPHATE AND FARNESYL RP DIPHOSPHATE, MUTAGENESIS OF PHE-112 AND PHE-113, AND SUBUNIT. RC TISSUE=Liver; RX PubMed=8986756; DOI=10.1073/pnas.93.26.15018; RA Tarshis L.C., Proteau P.J., Kellogg B.A., Sacchettini J.C., Poulter C.D.; RT "Regulation of product chain length by isoprenyl diphosphate synthases."; RL Proc. Natl. Acad. Sci. U.S.A. 93:15018-15023(1996). CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl CC pyrophosphate with the allylic pyrophosphates, dimethylallyl CC pyrophosphate, and then with the resultant geranylpyrophosphate to the CC ultimate product farnesyl pyrophosphate. CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate + dimethylallyl diphosphate = (2E)- CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, CC ChEBI:CHEBI:128769; EC=2.5.1.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate + (2E)-geranyl 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; CC Evidence={ECO:0000305|PubMed:8086404}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000305|PubMed:8086404}; CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; CC farnesyl diphosphate from geranyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8086404, CC ECO:0000269|PubMed:8986756}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 1FPS; X-ray; 2.60 A; A=20-367. DR PDB; 1UBV; X-ray; 2.50 A; A=1-367. DR PDB; 1UBW; X-ray; 2.50 A; A=1-367. DR PDB; 1UBX; X-ray; 2.50 A; A=1-367. DR PDB; 1UBY; X-ray; 2.40 A; A=1-367. DR AlphaFoldDB; P08836; -. DR MDposit; P08836; -. DR SMR; P08836; -. DR FunCoup; P08836; 2345. DR STRING; 9031.ENSGALP00000043372; -. DR PaxDb; 9031-ENSGALP00000043372; -. DR VEuPathDB; HostDB:geneid_425061; -. DR eggNOG; KOG0711; Eukaryota. DR InParanoid; P08836; -. DR OrthoDB; 10257492at2759; -. DR PhylomeDB; P08836; -. DR UniPathway; UPA00259; UER00368. DR UniPathway; UPA00260; UER00369. DR EvolutionaryTrace; P08836; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004337; F:(2E,6E)-farnesyl diphosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00685; Trans_IPPS_HT; 1. DR FunFam; 1.10.600.10:FF:000006; 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. PE 1: Evidence at protein level; KW 3D-structure; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm; KW Direct protein sequencing; Isoprene biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Magnesium; Metal-binding; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transferase. FT CHAIN 1..367 FT /note="Farnesyl pyrophosphate synthase" FT /id="PRO_0000123947" FT BINDING 71 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 74 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 110 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 121 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 121 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 126 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT BINDING 127 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 214 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT BINDING 215 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 254 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 271 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT SITE 112 FT /note="Important for determining product chain length" FT SITE 113 FT /note="Important for determining product chain length" FT MUTAGEN 112 FT /note="F->A: Alters selectivity towards product chain FT length, so that geranylgeranyl diphosphate is produced." FT /evidence="ECO:0000269|PubMed:8986756" FT MUTAGEN 113 FT /note="F->S: Alters selectivity towards product chain FT length, so that geranylfarnesyl diphosphate is produced." FT /evidence="ECO:0000269|PubMed:8986756" FT CONFLICT 191 FT /note="T -> G (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 201..203 FT /note="HFS -> TFQ (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 210..212 FT /note="IVK -> FVP (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 215..216 FT /note="TA -> AM (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 21..33 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 35..43 FT /evidence="ECO:0007829|PDB:1UBY" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:1UBY" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 53..66 FT /evidence="ECO:0007829|PDB:1UBY" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 73..85 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 93..121 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1UBY" FT TURN 136..140 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 141..161 FT /evidence="ECO:0007829|PDB:1UBY" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:1UBV" FT HELIX 167..191 FT /evidence="ECO:0007829|PDB:1UBY" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:1UBX" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:1UBX" FT HELIX 204..211 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 212..221 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 222..231 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 236..263 FT /evidence="ECO:0007829|PDB:1UBY" FT TURN 266..269 FT /evidence="ECO:0007829|PDB:1UBV" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 283..291 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:1UBY" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:1FPS" FT HELIX 309..322 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 324..346 FT /evidence="ECO:0007829|PDB:1UBY" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:1UBY" FT HELIX 353..362 FT /evidence="ECO:0007829|PDB:1UBY" SQ SEQUENCE 367 AA; 42153 MW; BB23D29D62CD842B CRC64; MHKFTGVNAK FQQPALRNLS PVVVEREREE FVGFFPQIVR DLTEDGIGHP EVGDAVARLK EVLQYNAPGG KCNRGLTVVA AYRELSGPGQ KDAESLRCAL AVGWCIELFQ AFFLVADDIM DQSLTRRGQL CWYKKEGVGL DAINDSFLLE SSVYRVLKKY CRQRPYYVHL LELFLQTAYQ TELGQMLDLI TAPVSKVDLS HFSEERYKAI VKYKTAFYSF YLPVAAAMYM VGIDSKEEHE NAKAILLEMG EYFQIQDDYL DCFGDPALTG KVGTDIQDNK CSWLVVQCLQ RVTPEQRQLL EDNYGRKEPE KVAKVKELYE AVGMRAAFQQ YEESSYRRLQ ELIEKHSNRL PKEIFLGLAQ KIYKRQK //