FPPS_CHICK
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 03-AUG-2022, entry version 120.
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=dimethylallyl diphosphate + isopentenyl 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=(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;
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}.
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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 PDBsum; 1FPS; -.
DR PDBsum; 1UBV; -.
DR PDBsum; 1UBW; -.
DR PDBsum; 1UBX; -.
DR PDBsum; 1UBY; -.
DR AlphaFoldDB; P08836; -.
DR SMR; P08836; -.
DR STRING; 9031.ENSGALP00000043372; -.
DR PRIDE; P08836; -.
DR VEuPathDB; HostDB:geneid_425061; -.
DR eggNOG; KOG0711; Eukaryota.
DR InParanoid; P08836; -.
DR PhylomeDB; P08836; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR EvolutionaryTrace; P08836; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IBA:GO_Central.
DR GO; GO:0004337; F:geranyltranstransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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 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..214
FT /evidence="ECO:0007829|PDB:1UBY"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1UBY"
FT HELIX 221..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
