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   25-NOV-2008, entry version 67.
DE   RecName: Full=Farnesyl pyrophosphate synthetase;
DE            Short=FPP synthetase;
DE            Short=FPS;
DE   AltName: Full=Farnesyl diphosphate synthetase;
DE   Includes:
DE     RecName: Full=Dimethylallyltranstransferase;
DE              EC=2.5.1.1;
DE   Includes:
DE     RecName: Full=Geranyltranstransferase;
DE              EC=2.5.1.10;
GN   Name=FDPS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE OF 187-216.
RC   TISSUE=Liver;
RX   MEDLINE=82000466; PubMed=7272273; DOI=10.1021/bi00516a007;
RA   Brems D.N., Bruenger E., Rillings H.C.;
RT   "Isolation and characterization of a photoaffinity-labeled peptide
RT   from the catalytic site of prenyltransferase.";
RL   Biochemistry 20:3711-3718(1981).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-367.
RC   TISSUE=Liver;
RX   MEDLINE=94368786; 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
RT   2.6-A resolution.";
RL   Biochemistry 33:10871-10877(1994).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-367.
RC   TISSUE=Liver;
RX   MEDLINE=97140274; PubMed=8986756; DOI=10.1073/pnas.93.26.15018;
RA   Tarshis L.C., Proteau P.J., Kellogg B.A., Sacchettini J.C.,
RA   Poulter C.D.;
RT   "Regulation of product chain length by isoprenyl diphosphate
RT   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
CC       the ultimate product farnesyl pyrophosphate.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranyl diphosphate.
CC   -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC       = diphosphate + trans,trans-farnesyl diphosphate.
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl-PP biosynthesis;
CC       farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl-PP biosynthesis;
CC       geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   UniGene; Gga.42725; -.
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   HOGENOM; P08836; -.
DR   HOVERGEN; P08836; -.
DR   LinkHub; P08836; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR008949; Terpenoid_synth.
DR   Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHET_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHET_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cholesterol biosynthesis; Cytoplasm;
KW   Direct protein sequencing; Isoprene biosynthesis; Lipid synthesis;
KW   Steroid biosynthesis; Sterol biosynthesis; Transferase.
FT   CHAIN         1    367       Farnesyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123947.
FT   ACT_SITE    206    206
FT   CONFLICT    191    191       T -> G (in Ref. 1; AA sequence).
FT   CONFLICT    201    203       HFS -> TFQ (in Ref. 1; AA sequence).
FT   CONFLICT    210    212       IVK -> FVP (in Ref. 1; AA sequence).
FT   CONFLICT    215    216       TA -> AM (in Ref. 1; AA sequence).
FT   HELIX        21     33
FT   HELIX        35     43
FT   TURN         44     46
FT   TURN         50     52
FT   HELIX        53     66
FT   STRAND       67     70
FT   HELIX        73     85
FT   HELIX        88     90
FT   HELIX        93    121
FT   HELIX       132    134
FT   TURN        136    140
FT   HELIX       141    161
FT   HELIX       167    191
FT   HELIX       204    214
FT   HELIX       216    219
FT   HELIX       221    231
FT   HELIX       236    263
FT   STRAND      276    278
FT   HELIX       283    291
FT   HELIX       294    303
FT   HELIX       309    322
FT   HELIX       324    346
FT   STRAND      348    350
FT   HELIX       353    362
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
//