Farnesyl diphosphate synthase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P22939 (ISPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Farnesyl diphosphate synthase
Short name=FPP synthase
EC=2.5.1.10

Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Geranyltranstransferase

Gene names

Name:	ispA
Ordered Locus Names:	b0421, JW0411

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate.
Cofactor	Binds 3 magnesium ions per subunit. Ref.5
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the FPP/GGPP synthase family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	farnesyl diphosphate biosynthetic process Inferred from mutant phenotype PubMed 2676985. Source: EcoCyc geranyl diphosphate biosynthetic process Inferred from mutant phenotype PubMed 15809342. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dimethylallyltranstransferase activity Inferred from direct assay PubMed 15721807. Source: EcoCyc geranyltranstransferase activity Inferred from direct assay PubMed 15721807. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

Farnesyl diphosphate synthase

PRO_0000123982

Sites

Metal binding

Magnesium 1

Metal binding

Magnesium 2

Metal binding

Magnesium 1

Metal binding

Magnesium 2

Metal binding

223

Magnesium 3

Binding site

Isopentenyl diphosphate

Binding site

Isopentenyl diphosphate

Binding site

Isopentenyl diphosphate

Binding site

Geranyl diphosphate

Binding site

Isopentenyl diphosphate

Binding site

181

Geranyl diphosphate

Binding site

182

Geranyl diphosphate

Binding site

220

Geranyl diphosphate

Binding site

237

Geranyl diphosphate

Secondary structure

299

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P22939 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 15BADD5E135060CA
Show »

FASTA

299

32,160

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli." Fujisaki S., Hara H., Nishimura Y., Horiuchi K., Nishino T. J. Biochem. 108:995-1000(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Sequence of minutes 4-25 of Escherichia coli." 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. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis." Hosfield D.J., Zhang Y., Dougan D.R., Broun A., Tari L.W., Swanson R.V., Finn J. J. Biol. Chem. 279:8526-8529(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ISOPENTENYL DIPHOSPHATE AND DIMETHYLALLYL S-THIOLODIPHOSPHATE, SUBUNIT, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D00694 Genomic DNA. Translation: BAA00599.1.
U82664 Genomic DNA. Translation: AAB40177.1.
U00096 Genomic DNA. Translation: AAC73524.1.
AP009048 Genomic DNA. Translation: BAE76201.1.

PIR

JQ0665.

RefSeq

NP_414955.1. NC_000913.2.
YP_488713.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RQI	X-ray	2.42	A/B	1-299	[»]
1RQJ	X-ray	1.95	A/B	1-299	[»]

ProteinModelPortal

P22939.

SMR

P22939. Positions 1-299.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10044N.

IntAct

P22939. 16 interactions.

MINT

MINT-1233182.

STRING

511145.b0421.

2D gel databases

SWISS-2DPAGE

P22939.

Proteomic databases

PaxDb

P22939.

PRIDE

P22939.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73524; AAC73524; b0421.
BAE76201; BAE76201; BAE76201.

GeneID

12930843.
945064.

KEGG

ecj:Y75_p0409.
eco:b0421.

PATRIC

32115991. VBIEscCol129921_0437.

Organism-specific databases

EchoBASE

EB0503.

EcoGene

EG10508. ispA.

Phylogenomic databases

eggNOG

COG0142.

HOGENOM

HOG000009101.

K00795.

OMA

NITEECI.

ProtClustDB

PRK10581.

Enzyme and pathway databases

BioCyc

EcoCyc:FPPSYN-MONOMER.
ECOL316407:JW0411-MONOMER.
MetaCyc:FPPSYN-MONOMER.

BRENDA

2.5.1.1. 2026.

SABIO-RK

P22939.

Gene expression databases

Genevestigator

P22939.

Family and domain databases

Gene3D

1.10.600.10. 1 hit.

InterPro

IPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]

PANTHER

PTHR12001. PTHR12001. 1 hit.

Pfam

PF00348. polyprenyl_synt. 1 hit.
[Graphical view]

SUPFAM

SSF48576. Terpenoid_synth. 1 hit.

PROSITE

PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075078.

EvolutionaryTrace

P22939.

Entry information

Entry name

ISPA_ECOLI

Accession

Primary (citable) accession number: P22939
Secondary accession number(s): Q2MC05

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents