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Protein

Fructose-1,6-bisphosphatase class 1

Gene

fbp

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

Functioni

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+2 PublicationsNote: Binds 2 magnesium ions per subunit.2 Publications

Enzyme regulationi

Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. Activated by three-carbon carboxylic acids, phosphorylated three-carbon carboxylic acids and sulfate. Strongly activated by phosphoenolpyruvate and citrate. Inhibited by AMP, which affects the turnover of bound substrate and not the affinity for substrate. Allosterically inhibited by glucose 6-phosphate. AMP and glucose 6-phosphate act synergistically as allosteric inhibitors. Phosphoenolpyruvate antagonizes inhibition by AMP and glucose 6-phosphate. Fructose 2,6-bisphosphate acts as competitive inhibitor.4 Publications

Kineticsi

  1. KM=1.7 µM for fructose 1,6-biphosphate1 Publication

    Pathwayi: gluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei30 – 301Allosteric activator
    Metal bindingi89 – 891Magnesium 1
    Metal bindingi110 – 1101Magnesium 1
    Metal bindingi110 – 1101Magnesium 2
    Metal bindingi112 – 1121Magnesium 1; via carbonyl oxygen
    Metal bindingi113 – 1131Magnesium 2
    Binding sitei187 – 1871Allosteric activator; via amide nitrogen
    Binding sitei206 – 2061Substrate
    Binding sitei222 – 2221Allosteric inhibitor glucose-6-phosphate
    Binding sitei225 – 2251Allosteric inhibitor glucose-6-phosphate
    Binding sitei239 – 2391Substrate
    Binding sitei269 – 2691Substrate
    Metal bindingi275 – 2751Magnesium 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 235AMP1 Publication
    Nucleotide bindingi104 – 1052AMP1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • dephosphorylation Source: GOC
    • gluconeogenesis Source: EcoCyc
    • protein homotetramerization Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:F16B-MONOMER.
    ECOL316407:JW4191-MONOMER.
    MetaCyc:F16B-MONOMER.
    BRENDAi3.1.3.11. 2026.
    SABIO-RKP0A993.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase class 1 (EC:3.1.3.11)
    Short name:
    FBPase class 1
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
    Gene namesi
    Name:fbp
    Synonyms:fdp
    Ordered Locus Names:b4232, JW4191
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10283. fbp.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Fructose-1,6-bisphosphatase class 1PRO_0000200492Add
    BLAST

    Proteomic databases

    EPDiP0A993.
    PaxDbiP0A993.
    PRIDEiP0A993.

    2D gel databases

    SWISS-2DPAGEP0A993.

    Interactioni

    Subunit structurei

    Homotetramer. Phosphoenolpyruvate stabilizes the homotetramer.4 Publications

    Protein-protein interaction databases

    BioGridi4259316. 10 interactions.
    STRINGi511145.b4232.

    Structurei

    Secondary structure

    1
    332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107Combined sources
    Turni11 – 144Combined sources
    Helixi15 – 173Combined sources
    Helixi19 – 4022Combined sources
    Turni41 – 488Combined sources
    Beta strandi50 – 556Combined sources
    Beta strandi61 – 633Combined sources
    Helixi65 – 7915Combined sources
    Beta strandi83 – 886Combined sources
    Beta strandi105 – 1139Combined sources
    Helixi115 – 1206Combined sources
    Beta strandi124 – 1329Combined sources
    Helixi143 – 1464Combined sources
    Helixi150 – 1523Combined sources
    Beta strandi154 – 17320Combined sources
    Beta strandi175 – 1806Combined sources
    Turni182 – 1843Combined sources
    Beta strandi186 – 1949Combined sources
    Beta strandi202 – 2043Combined sources
    Helixi207 – 2126Combined sources
    Helixi215 – 22410Combined sources
    Helixi229 – 2313Combined sources
    Helixi243 – 25311Combined sources
    Beta strandi256 – 2594Combined sources
    Beta strandi263 – 2653Combined sources
    Beta strandi269 – 2713Combined sources
    Turni272 – 2754Combined sources
    Helixi276 – 28510Combined sources
    Beta strandi289 – 2968Combined sources
    Helixi297 – 2993Combined sources
    Beta strandi311 – 3155Combined sources
    Helixi316 – 32813Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GQ1X-ray1.45A1-332[»]
    2OWZX-ray2.18A1-332[»]
    2OX3X-ray2.18A1-332[»]
    2Q8MX-ray2.05A/B1-332[»]
    2QVRX-ray2.18A1-332[»]
    ProteinModelPortaliP0A993.
    SMRiP0A993. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A993.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3 – 53Allosteric activator binding
    Regioni113 – 1164Substrate binding
    Regioni257 – 2593Substrate binding

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CZI. Bacteria.
    COG0158. LUCA.
    HOGENOMiHOG000191265.
    InParanoidiP0A993.
    KOiK03841.
    OMAiYTTRYIG.
    OrthoDBiEOG6X10TR.
    PhylomeDBiP0A993.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1.
    IPR033391. FBPase_N.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A993-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTLGEFIVE KQHEFSHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG
    60 70 80 90 100
    ASGAENVQGE VQQKLDLFAN EKLKAALKAR DIVAGIASEE EDEIVVFEGC
    110 120 130 140 150
    EHAKYVVLMD PLDGSSNIDV NVSVGTIFSI YRRVTPVGTP VTEEDFLQPG
    160 170 180 190 200
    NKQVAAGYVV YGSSTMLVYT TGCGVHAFTY DPSLGVFCLC QERMRFPEKG
    210 220 230 240 250
    KTYSINEGNY IKFPNGVKKY IKFCQEEDKS TNRPYTSRYI GSLVADFHRN
    260 270 280 290 300
    LLKGGIYLYP STASHPDGKL RLLYECNPMA FLAEQAGGKA SDGKERILDI
    310 320 330
    IPETLHQRRS FFVGNDHMVE DVERFIREFP DA
    Length:332
    Mass (Da):36,834
    Last modified:July 19, 2005 - v1
    Checksum:i4F0FC8109491D78F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X12545 mRNA. Translation: CAA31062.1.
    U14003 Genomic DNA. Translation: AAA97129.1.
    U00096 Genomic DNA. Translation: AAC77189.1.
    AP009048 Genomic DNA. Translation: BAE78232.1.
    PIRiS01383. PAEC.
    RefSeqiNP_418653.1. NC_000913.3.
    WP_000853753.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77189; AAC77189; b4232.
    BAE78232; BAE78232; BAE78232.
    GeneIDi948753.
    KEGGiecj:JW4191.
    eco:b4232.
    PATRICi32124037. VBIEscCol129921_4363.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X12545 mRNA. Translation: CAA31062.1.
    U14003 Genomic DNA. Translation: AAA97129.1.
    U00096 Genomic DNA. Translation: AAC77189.1.
    AP009048 Genomic DNA. Translation: BAE78232.1.
    PIRiS01383. PAEC.
    RefSeqiNP_418653.1. NC_000913.3.
    WP_000853753.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GQ1X-ray1.45A1-332[»]
    2OWZX-ray2.18A1-332[»]
    2OX3X-ray2.18A1-332[»]
    2Q8MX-ray2.05A/B1-332[»]
    2QVRX-ray2.18A1-332[»]
    ProteinModelPortaliP0A993.
    SMRiP0A993. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259316. 10 interactions.
    STRINGi511145.b4232.

    2D gel databases

    SWISS-2DPAGEP0A993.

    Proteomic databases

    EPDiP0A993.
    PaxDbiP0A993.
    PRIDEiP0A993.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77189; AAC77189; b4232.
    BAE78232; BAE78232; BAE78232.
    GeneIDi948753.
    KEGGiecj:JW4191.
    eco:b4232.
    PATRICi32124037. VBIEscCol129921_4363.

    Organism-specific databases

    EchoBASEiEB0279.
    EcoGeneiEG10283. fbp.

    Phylogenomic databases

    eggNOGiENOG4105CZI. Bacteria.
    COG0158. LUCA.
    HOGENOMiHOG000191265.
    InParanoidiP0A993.
    KOiK03841.
    OMAiYTTRYIG.
    OrthoDBiEOG6X10TR.
    PhylomeDBiP0A993.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BioCyciEcoCyc:F16B-MONOMER.
    ECOL316407:JW4191-MONOMER.
    MetaCyc:F16B-MONOMER.
    BRENDAi3.1.3.11. 2026.
    SABIO-RKP0A993.

    Miscellaneous databases

    EvolutionaryTraceiP0A993.
    PROiP0A993.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1.
    IPR033391. FBPase_N.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene."
      Hamilton W.D.O., Harrison D.A., Dyer T.A.
      Nucleic Acids Res. 16:8707-8707(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      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. "Amino acid sequence homology among fructose-1,6-bisphosphatases."
      Marcus F., Gontero B., Harrsch P.B., Rittenhouse J.
      Biochem. Biophys. Res. Commun. 135:374-381(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 43-62; 220-229; 239-249; 254-269 AND 297-308.
    6. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    7. "Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase."
      Hines J.K., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 281:18386-18393(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SULFATE IONS, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    8. "Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state."
      Hines J.K., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 282:11696-11704(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; CITRATE AND PHOSPHOENOLPYRUVATE, ENZYME REGULATION, SUBUNIT.
    9. "Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch."
      Hines J.K., Kruesel C.E., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 282:24697-24706(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-1,6-BIPHOSPHATE; MAGNESIUM IONS; AMP AND GLUCOSE-6-PHOSPHATE, SUBUNIT, COFACTOR, ENZYME REGULATION.
    10. "Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition."
      Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 282:36121-36131(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BIPHOSPHATE; MAGNESIUM IONS AND CITRATE, ENZYME REGULATION.

    Entry informationi

    Entry nameiF16PA_ECOLI
    AccessioniPrimary (citable) accession number: P0A993
    Secondary accession number(s): P09200, Q2M674
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: May 11, 2016
    This is version 101 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    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 one 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.