[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=2089044 [NCBI, ExPASy, EBI, Israel, Japan] Fujisaki S., Hara H., Nishimura Y., Horiuchi K., Nishino T.; "Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli."; J. Biochem. 108:995-1000(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the FPP/GGPP synthetase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D00694; BAA00599.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U82664; AAB40177.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73524.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76201.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ0665; JQ0665.

RefSeq

AP_001071.1; -.
NP_414955.1; -.

3D structure databases

PDB

1RQI; X-ray; 2.42 A; A/B=1-299.	[ExPASy / RCSB / EBI]
1RQJ; X-ray; 1.95 A; A/B=1-299.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1RQI; -.
1RQJ; -.

ModBase

P22939.

Protein-protein interaction databases

DIP

DIP:10044N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:FPPSYN-MON; -.
MetaCyc:FPPSYN-MON; -.

2D gel databases

SWISS-2DPAGE

P22939; -.

Organism-specific databases

EchoBASE

EB0503; -.

EcoGene

EG10508; ispA.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004337;	Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
GO:0008299;	Biological process: isoprenoid biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000092; Polyprenyl_synt.
IPR017446; Polyprenyl_synth-rel.
IPR008949; Terpenoid_synth.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.600.10; Terpenoid_synth; 1.

PANTHER

PTHR12001; Polyprenyl_synt; 1.

Pfam

PF00348; polyprenyl_synt; 1.
Pfam graphical view of domain structure.

PROSITE

PS00723; POLYPRENYL_SYNTHET_1; 1.
PS00444; POLYPRENYL_SYNTHET_2; 1.

ProtoNet

P22939.

Genome annotation databases

GeneID

945064; -.

GenomeReviews

U00096_GR; b0421.
AP009048_GR; JW0411.

KEGG

ecj:JW0411; -.
eco:b0421; -.

Phylogenomic databases

HOGENOM

P22939; -.

Genome annotation databases

CMR

P22939; b0421.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Cytoplasm; Isoprene biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 299`	`299`	`Geranyltranstransferase.`	`PRO_0000123982`
`HELIX`	`3 22`	`20`
`STRAND`	`25 27`	`3`
`HELIX`	`31 41`	`11`
`HELIX`	`47 58`	`12`
`HELIX`	`63 84`	`22`
`TURN`	`87 90`	`4`
`HELIX`	`101 105`	`5`
`HELIX`	`107 127`	`21`
`HELIX`	`135 149`	`15`
`HELIX`	`154 163`	`10`
`TURN`	`164 167`	`4`
`HELIX`	`171 181`	`11`
`HELIX`	`183 195`	`13`
`TURN`	`196 198`	`3`
`HELIX`	`199 203`	`5`
`HELIX`	`205 229`	`25`
`HELIX`	`232 235`	`4`
`HELIX`	`241 245`	`5`
`HELIX`	`250 278`	`29`
`TURN`	`279 281`	`3`
`HELIX`	`285 296`	`12`

Sequence information

Length: 299 AA [This is the length of the unprocessed precursor]

Molecular weight: 32160 Da [This is the MW of the unprocessed precursor]

CRC64: 15BADD5E135060CA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDFPQQLEAC VKQANQALSR FIAPLPFQNT PVVETMQYGA LLGGKRLRPF LVYATGHMFG 

        70         80         90        100        110        120 
VSTNTLDAPA AAVECIHAYS LIHDDLPAMD DDDLRRGLPT CHVKFGEANA ILAGDALQTL 

       130        140        150        160        170        180 
AFSILSDADM PEVSDRDRIS MISELASASG IAGMCGGQAL DLDAEGKHVP LDALERIHRH 

       190        200        210        220        230        240 
KTGALIRAAV RLGALSAGDK GRRALPVLDK YAESIGLAFQ VQDDILDVVG DTATLGKRQG 

       250        260        270        280        290 
ADQQLGKSTY PALLGLEQAR KKARDLIDDA RQSLKQLAEQ SLDTSALEAL ADYIIQRNK

P22939 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools