Reviewed, UniProtKB/Swiss-Prot P08836 (FPPS_CHICK)

Names and origin

Protein names

Recommended name:
    Farnesyl pyrophosphate synthetase
      Short name=FPP synthetase
      Short name=FPS
Alternative name(s):
    Farnesyl diphosphate synthetase
Including the following 2 domains:
    1- Recommended name:
            Dimethylallyltranstransferase
              EC=2.5.1.1
    2- Recommended name:
            Geranyltranstransferase
              EC=2.5.1.10

Gene names

Name:

FDPS

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Catalytic activity	Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.
Pathway	Isoprenoid biosynthesis; farnesyl-PP biosynthesis; farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1. Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the FPP/GGPP synthetase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 367

367

Farnesyl pyrophosphate synthetase

Sites

Active site

206

1

Experimental info

Sequence conflict

191

1

T → G AA sequence Ref.1

Sequence conflict

201 – 203

3

HFS → TFQ AA sequence Ref.1

Sequence conflict

210 – 212

3

IVK → FVP AA sequence Ref.1

Sequence conflict

215 – 216

2

TA → AM AA sequence Ref.1

Secondary structure

1

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367

Helix Strand Turn

Details...

Helix

21 – 33

13

Helix

35 – 43

9

Turn

44 – 46

3

Turn

50 – 52

3

Helix

53 – 66

14

Beta strand

67 – 70

4

Helix

73 – 85

13

Helix

88 – 90

3

Helix

93 – 121

29

Helix

132 – 134

3

Turn

136 – 140

5

Helix

141 – 161

21

Helix

167 – 191

25

Helix

204 – 214

11

Helix

216 – 219

4

Helix

221 – 231

11

Helix

236 – 263

28

Beta strand

276 – 278

3

Helix

283 – 291

9

Helix

294 – 303

10

Helix

309 – 322

14

Helix

324 – 346

23

Beta strand

348 – 350

3

Helix

353 – 362

10

Sequences

	Sequence		Length	Mass (Da)
	P08836-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: BB23D29D62CD842B	FASTA	367	42,153
	10 20 30 40 50 60 MHKFTGVNAK FQQPALRNLS PVVVEREREE FVGFFPQIVR DLTEDGIGHP EVGDAVARLK 70 80 90 100 110 120 EVLQYNAPGG KCNRGLTVVA AYRELSGPGQ KDAESLRCAL AVGWCIELFQ AFFLVADDIM 130 140 150 160 170 180 DQSLTRRGQL CWYKKEGVGL DAINDSFLLE SSVYRVLKKY CRQRPYYVHL LELFLQTAYQ 190 200 210 220 230 240 TELGQMLDLI TAPVSKVDLS HFSEERYKAI VKYKTAFYSF YLPVAAAMYM VGIDSKEEHE 250 260 270 280 290 300 NAKAILLEMG EYFQIQDDYL DCFGDPALTG KVGTDIQDNK CSWLVVQCLQ RVTPEQRQLL 310 320 330 340 350 360 EDNYGRKEPE KVAKVKELYE AVGMRAAFQQ YEESSYRRLQ ELIEKHSNRL PKEIFLGLAQ KIYKRQK

References

[1]	"Isolation and characterization of a photoaffinity-labeled peptide from the catalytic site of prenyltransferase." Brems D.N., Bruenger E., Rillings H.C. Biochemistry 20:3711-3718(1981) [PubMed: 7272273] [Abstract] Cited for: PROTEIN SEQUENCE OF 187-216. Tissue: Liver.
[2]	"Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution." Tarshis L.C., Yan M., Poulter C.D., Sacchettini J.C. Biochemistry 33:10871-10877(1994) [PubMed: 8086404] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-367. Tissue: Liver.
[3]	"Regulation of product chain length by isoprenyl diphosphate synthases." Tarshis L.C., Proteau P.J., Kellogg B.A., Sacchettini J.C., Poulter C.D. Proc. Natl. Acad. Sci. U.S.A. 93:15018-15023(1996) [PubMed: 8986756] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-367. Tissue: Liver.

Cross-references

Sequence databases

UniGene

Gga.42725

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FPS	X-ray	2.60	A	20-367	[»]
1UBV	X-ray	2.50	A	1-367	[»]
1UBW	X-ray	2.50	A	1-367	[»]
1UBX	X-ray	2.50	A	1-367	[»]
1UBY	X-ray	2.40	A	1-367	[»]

ModBase

Search...

Phylogenomic databases

HOGENOM

P08836.

HOVERGEN

P08836.

Family and domain databases

InterPro

IPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]

Gene3D

G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.

Pfam

PF00348. polyprenyl_synt. 1 hit.
[Graphical view]

PROSITE

PS00723. POLYPRENYL_SYNTHET_1. 1 hit.
PS00444. POLYPRENYL_SYNTHET_2. 1 hit.
[Graphical view]

ProDom

P08836.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

LinkHub

P08836.

ProtoNet

Search...

Entry information

Entry name

FPPS_CHICK

Accession

Primary (citable) accession number: P08836

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	December 15, 1998
Last modified:	September 2, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)