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P22939 (ISPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Farnesyl diphosphate synthase
PRO_0000123982

Sites

Metal binding841Magnesium 1
Metal binding841Magnesium 2
Metal binding901Magnesium 1
Metal binding901Magnesium 2
Metal binding2231Magnesium 3
Binding site451Isopentenyl diphosphate
Binding site481Isopentenyl diphosphate
Binding site771Isopentenyl diphosphate
Binding site951Geranyl diphosphate
Binding site961Isopentenyl diphosphate
Binding site1811Geranyl diphosphate
Binding site1821Geranyl diphosphate
Binding site2201Geranyl diphosphate
Binding site2371Geranyl diphosphate

Secondary structure

....................................... 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22939 [UniParc].

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

FASTA29932,160
        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' 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 277:1453-1462(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.
PIRJQ0665.
RefSeqNP_414955.1. NC_000913.3.
YP_488713.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RQIX-ray2.42A/B1-299[»]
1RQJX-ray1.95A/B1-299[»]
ProteinModelPortalP22939.
SMRP22939. Positions 1-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10044N.
IntActP22939. 16 interactions.
MINTMINT-1233182.
STRING511145.b0421.

Chemistry

ChEMBLCHEMBL1075078.

2D gel databases

SWISS-2DPAGEP22939.

Proteomic databases

PaxDbP22939.
PRIDEP22939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73524; AAC73524; b0421.
BAE76201; BAE76201; BAE76201.
GeneID12930843.
945064.
KEGGecj:Y75_p0409.
eco:b0421.
PATRIC32115991. VBIEscCol129921_0437.

Organism-specific databases

EchoBASEEB0503.
EcoGeneEG10508. ispA.

Phylogenomic databases

eggNOGCOG0142.
HOGENOMHOG000009101.
KOK00795.
OMAGHFSEEL.
OrthoDBEOG6TN43W.
PhylomeDBP22939.

Enzyme and pathway databases

BioCycEcoCyc:FPPSYN-MONOMER.
ECOL316407:JW0411-MONOMER.
MetaCyc:FPPSYN-MONOMER.
BRENDA2.5.1.1. 2026.
SABIO-RKP22939.

Gene expression databases

GenevestigatorP22939.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
PANTHERPTHR12001. PTHR12001. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22939.
PROP22939.

Entry information

Entry nameISPA_ECOLI
AccessionPrimary (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: June 11, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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