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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)DescriptionActionsGraphical viewLength
    Binding sitei30Allosteric activator1
    Metal bindingi89Magnesium 11
    Metal bindingi110Magnesium 11
    Metal bindingi110Magnesium 21
    Metal bindingi112Magnesium 1; via carbonyl oxygen1
    Metal bindingi113Magnesium 21
    Binding sitei187Allosteric activator; via amide nitrogen1
    Binding sitei206Substrate1
    Binding sitei222Allosteric inhibitor glucose-6-phosphate1
    Binding sitei225Allosteric inhibitor glucose-6-phosphate1
    Binding sitei239Substrate1
    Binding sitei269Substrate1
    Metal bindingi275Magnesium 21

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi19 – 23AMP1 Publication5
    Nucleotide bindingi104 – 105AMP1 Publication2

    GO - Molecular functioni

    GO - Biological processi

    • fructose 1,6-bisphosphate metabolic process Source: GO_Central
    • fructose 6-phosphate metabolic process Source: GO_Central
    • fructose catabolic process Source: InterPro
    • fructose metabolic process Source: GO_Central
    • gluconeogenesis Source: EcoCyc
    • protein homotetramerization Source: EcoCyc
    • sucrose biosynthetic process Source: GO_Central
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00002004921 – 332Fructose-1,6-bisphosphatase class 1Add BLAST332

    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 interactors.
    STRINGi511145.b4232.

    Structurei

    Secondary structure

    1332
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 10Combined sources7
    Turni11 – 14Combined sources4
    Helixi15 – 17Combined sources3
    Helixi19 – 40Combined sources22
    Turni41 – 48Combined sources8
    Beta strandi50 – 55Combined sources6
    Beta strandi61 – 63Combined sources3
    Helixi65 – 79Combined sources15
    Beta strandi83 – 88Combined sources6
    Beta strandi105 – 113Combined sources9
    Helixi115 – 120Combined sources6
    Beta strandi124 – 132Combined sources9
    Helixi143 – 146Combined sources4
    Helixi150 – 152Combined sources3
    Beta strandi154 – 173Combined sources20
    Beta strandi175 – 180Combined sources6
    Turni182 – 184Combined sources3
    Beta strandi186 – 194Combined sources9
    Beta strandi202 – 204Combined sources3
    Helixi207 – 212Combined sources6
    Helixi215 – 224Combined sources10
    Helixi229 – 231Combined sources3
    Helixi243 – 253Combined sources11
    Beta strandi256 – 259Combined sources4
    Beta strandi263 – 265Combined sources3
    Beta strandi269 – 271Combined sources3
    Turni272 – 275Combined sources4
    Helixi276 – 285Combined sources10
    Beta strandi289 – 296Combined sources8
    Helixi297 – 299Combined sources3
    Beta strandi311 – 315Combined sources5
    Helixi316 – 328Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A993.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni3 – 5Allosteric activator binding3
    Regioni113 – 116Substrate binding4
    Regioni257 – 259Substrate binding3

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

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

    Family and domain databases

    CDDicd00354. FBPase. 1 hit.
    HAMAPiMF_01855. FBPase_class1. 1 hit.
    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259316. 10 interactors.
    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.
    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

    CDDicd00354. FBPase. 1 hit.
    HAMAPiMF_01855. FBPase_class1. 1 hit.
    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...

    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: November 2, 2016
    This is version 105 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.