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Protein

Farnesyl diphosphate synthase

Gene

ispA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate.

Cofactori

Mg2+1 PublicationNote: Binds 3 Mg2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451Isopentenyl diphosphate1 Publication
Binding sitei48 – 481Isopentenyl diphosphate1 Publication
Binding sitei77 – 771Isopentenyl diphosphate1 Publication
Metal bindingi84 – 841Magnesium 11 Publication
Metal bindingi84 – 841Magnesium 21 Publication
Metal bindingi90 – 901Magnesium 11 Publication
Metal bindingi90 – 901Magnesium 21 Publication
Binding sitei95 – 951Geranyl diphosphate
Binding sitei96 – 961Isopentenyl diphosphate1 Publication
Binding sitei181 – 1811Geranyl diphosphate
Binding sitei182 – 1821Geranyl diphosphate
Binding sitei220 – 2201Geranyl diphosphate
Metal bindingi223 – 2231Magnesium 31 Publication
Binding sitei237 – 2371Geranyl diphosphate

GO - Molecular functioni

  • dimethylallyltranstransferase activity Source: EcoCyc
  • geranyltranstransferase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • farnesyl diphosphate biosynthetic process Source: EcoCyc
  • geranyl diphosphate biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Isoprene biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FPPSYN-MONOMER.
ECOL316407:JW0411-MONOMER.
MetaCyc:FPPSYN-MONOMER.
SABIO-RKP22939.

Names & Taxonomyi

Protein namesi
Recommended name:
Farnesyl diphosphate synthase (EC:2.5.1.10)
Short name:
FPP synthase
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Geranyltranstransferase
Gene namesi
Name:ispA
Ordered Locus Names:b0421, JW0411
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10508. ispA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Farnesyl diphosphate synthasePRO_0000123982Add
BLAST

Proteomic databases

PaxDbiP22939.
PRIDEiP22939.

2D gel databases

SWISS-2DPAGEP22939.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
flxAP776095EBI-553011,EBI-553024
purTP332213EBI-553011,EBI-553029

Protein-protein interaction databases

DIPiDIP-10044N.
IntActiP22939. 16 interactions.
MINTiMINT-1233182.
STRINGi511145.b0421.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2220Combined sources
Beta strandi25 – 273Combined sources
Helixi31 – 4111Combined sources
Helixi47 – 5812Combined sources
Helixi63 – 8422Combined sources
Turni87 – 904Combined sources
Helixi101 – 1055Combined sources
Helixi107 – 12721Combined sources
Helixi135 – 14915Combined sources
Helixi154 – 16310Combined sources
Turni164 – 1674Combined sources
Helixi171 – 18111Combined sources
Helixi183 – 19513Combined sources
Turni196 – 1983Combined sources
Helixi199 – 22931Combined sources
Helixi232 – 2354Combined sources
Helixi241 – 2455Combined sources
Helixi250 – 2545Combined sources
Helixi256 – 27823Combined sources
Turni279 – 2813Combined sources
Helixi285 – 29612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RQIX-ray2.42A/B1-299[»]
1RQJX-ray1.95A/B1-299[»]
ProteinModelPortaliP22939.
SMRiP22939. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22939.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Phylogenomic databases

eggNOGiCOG0142.
HOGENOMiHOG000009101.
InParanoidiP22939.
KOiK00795.
OMAiGHFSEEL.
OrthoDBiEOG6TN43W.
PhylomeDBiP22939.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
[Graphical view]
PANTHERiPTHR12001. PTHR12001. 1 hit.
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFPQQLEAC VKQANQALSR FIAPLPFQNT PVVETMQYGA LLGGKRLRPF
60 70 80 90 100
LVYATGHMFG VSTNTLDAPA AAVECIHAYS LIHDDLPAMD DDDLRRGLPT
110 120 130 140 150
CHVKFGEANA ILAGDALQTL AFSILSDADM PEVSDRDRIS MISELASASG
160 170 180 190 200
IAGMCGGQAL DLDAEGKHVP LDALERIHRH KTGALIRAAV RLGALSAGDK
210 220 230 240 250
GRRALPVLDK YAESIGLAFQ VQDDILDVVG DTATLGKRQG ADQQLGKSTY
260 270 280 290
PALLGLEQAR KKARDLIDDA RQSLKQLAEQ SLDTSALEAL ADYIIQRNK
Length:299
Mass (Da):32,160
Last modified:August 1, 1991 - v1
Checksum:i15BADD5E135060CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00694 Genomic DNA. Translation: BAA00599.1.
U82664 Genomic DNA. Translation: AAB40177.1.
U00096 Genomic DNA. Translation: AAC73524.1.
AP009048 Genomic DNA. Translation: BAE76201.1.
PIRiJQ0665.
RefSeqiNP_414955.1. NC_000913.3.
WP_000347217.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC73524; AAC73524; b0421.
BAE76201; BAE76201; BAE76201.
GeneIDi945064.
KEGGieco:b0421.
PATRICi32115991. VBIEscCol129921_0437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00694 Genomic DNA. Translation: BAA00599.1.
U82664 Genomic DNA. Translation: AAB40177.1.
U00096 Genomic DNA. Translation: AAC73524.1.
AP009048 Genomic DNA. Translation: BAE76201.1.
PIRiJQ0665.
RefSeqiNP_414955.1. NC_000913.3.
WP_000347217.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RQIX-ray2.42A/B1-299[»]
1RQJX-ray1.95A/B1-299[»]
ProteinModelPortaliP22939.
SMRiP22939. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10044N.
IntActiP22939. 16 interactions.
MINTiMINT-1233182.
STRINGi511145.b0421.

Chemistry

ChEMBLiCHEMBL1075078.

2D gel databases

SWISS-2DPAGEP22939.

Proteomic databases

PaxDbiP22939.
PRIDEiP22939.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73524; AAC73524; b0421.
BAE76201; BAE76201; BAE76201.
GeneIDi945064.
KEGGieco:b0421.
PATRICi32115991. VBIEscCol129921_0437.

Organism-specific databases

EchoBASEiEB0503.
EcoGeneiEG10508. ispA.

Phylogenomic databases

eggNOGiCOG0142.
HOGENOMiHOG000009101.
InParanoidiP22939.
KOiK00795.
OMAiGHFSEEL.
OrthoDBiEOG6TN43W.
PhylomeDBiP22939.

Enzyme and pathway databases

BioCyciEcoCyc:FPPSYN-MONOMER.
ECOL316407:JW0411-MONOMER.
MetaCyc:FPPSYN-MONOMER.
SABIO-RKP22939.

Miscellaneous databases

EvolutionaryTraceiP22939.
PROiP22939.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
[Graphical view]
PANTHERiPTHR12001. PTHR12001. 1 hit.
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiISPA_ECOLI
AccessioniPrimary (citable) accession number: P22939
Secondary accession number(s): Q2MC05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 22, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.