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P22939

- ISPA_ECOLI

UniProt

P22939 - ISPA_ECOLI

Protein

Farnesyl diphosphate synthase

Gene

ispA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 3 magnesium 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

    1. dimethylallyltranstransferase activity Source: EcoCyc
    2. geranyltranstransferase activity Source: EcoCyc
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. farnesyl diphosphate biosynthetic process Source: EcoCyc
    2. geranyl diphosphate biosynthetic process Source: EcoCyc

    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.
    BRENDAi2.5.1.1. 2026.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10508. ispA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP22939.

    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 – 2220
    Beta strandi25 – 273
    Helixi31 – 4111
    Helixi47 – 5812
    Helixi63 – 8422
    Turni87 – 904
    Helixi101 – 1055
    Helixi107 – 12721
    Helixi135 – 14915
    Helixi154 – 16310
    Turni164 – 1674
    Helixi171 – 18111
    Helixi183 – 19513
    Turni196 – 1983
    Helixi199 – 22931
    Helixi232 – 2354
    Helixi241 – 2455
    Helixi250 – 2545
    Helixi256 – 27823
    Turni279 – 2813
    Helixi285 – 29612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00795.
    OMAiGHFSEEL.
    OrthoDBiEOG6TN43W.
    PhylomeDBiP22939.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [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

    MDFPQQLEAC VKQANQALSR FIAPLPFQNT PVVETMQYGA LLGGKRLRPF    50
    LVYATGHMFG VSTNTLDAPA AAVECIHAYS LIHDDLPAMD DDDLRRGLPT 100
    CHVKFGEANA ILAGDALQTL AFSILSDADM PEVSDRDRIS MISELASASG 150
    IAGMCGGQAL DLDAEGKHVP LDALERIHRH KTGALIRAAV RLGALSAGDK 200
    GRRALPVLDK YAESIGLAFQ VQDDILDVVG DTATLGKRQG ADQQLGKSTY 250
    PALLGLEQAR KKARDLIDDA RQSLKQLAEQ SLDTSALEAL ADYIIQRNK 299
    Length:299
    Mass (Da):32,160
    Last modified:August 1, 1991 - v1
    Checksum:i15BADD5E135060CA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488713.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73524; AAC73524; b0421.
    BAE76201; BAE76201; BAE76201.
    GeneIDi12930843.
    945064.
    KEGGiecj:Y75_p0409.
    eco:b0421.
    PATRICi32115991. VBIEscCol129921_0437.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi JQ0665.
    RefSeqi NP_414955.1. NC_000913.3.
    YP_488713.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P22939.
    SMRi P22939. Positions 1-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10044N.
    IntActi P22939. 16 interactions.
    MINTi MINT-1233182.
    STRINGi 511145.b0421.

    Chemistry

    ChEMBLi CHEMBL1075078.

    2D gel databases

    SWISS-2DPAGE P22939.

    Proteomic databases

    PaxDbi P22939.
    PRIDEi P22939.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73524 ; AAC73524 ; b0421 .
    BAE76201 ; BAE76201 ; BAE76201 .
    GeneIDi 12930843.
    945064.
    KEGGi ecj:Y75_p0409.
    eco:b0421.
    PATRICi 32115991. VBIEscCol129921_0437.

    Organism-specific databases

    EchoBASEi EB0503.
    EcoGenei EG10508. ispA.

    Phylogenomic databases

    eggNOGi COG0142.
    HOGENOMi HOG000009101.
    KOi K00795.
    OMAi GHFSEEL.
    OrthoDBi EOG6TN43W.
    PhylomeDBi P22939.

    Enzyme and pathway databases

    BioCyci EcoCyc:FPPSYN-MONOMER.
    ECOL316407:JW0411-MONOMER.
    MetaCyc:FPPSYN-MONOMER.
    BRENDAi 2.5.1.1. 2026.
    SABIO-RK P22939.

    Miscellaneous databases

    EvolutionaryTracei P22939.
    PROi P22939.

    Gene expression databases

    Genevestigatori P22939.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    PANTHERi PTHR12001. PTHR12001. 1 hit.
    Pfami PF00348. polyprenyl_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    PROSITEi PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
    PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 121 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