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UniProtKB - P06999 (PFKB_ECOLI)

Entry version 163 (05 Jun 2019)
Sequence version 2 (01 Nov 1997)
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Protein

ATP-dependent 6-phosphofructokinase isozyme 2

Gene

pfkB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.1 Publication

Miscellaneous

Only 10% of the activity present in the wild-type strain is phosphofructokinase-2.
This enzyme is not to be confused with 6-phosphofructo-2-kinase which is also called phosphofructokinase 2.
E.coli has two 6-phosphofructokinases enzymes.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically inhibited by ATP. Allosteric ATP-binding requires the presence of the substrate ATP. Inhibited by monovalent cations with ionic radii larger than Na+ (e.g. K+, Cs+). The monovalent cations increase the affinity of the allosteric site for ATP. PFK-2 is sensitive to inhibition by fructose 1,6-diphosphate.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=8 µM for ATP1 Publication
  2. KM=6 µM for fructose 6-phosphate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

    This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Glucose-6-phosphate isomerase (pgi)
    3. ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA), ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB)
    4. Fructose-bisphosphate aldolase class 2 (fbaA)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei27Allosteric inhibitor ATP; shared with dimeric partner1 Publication1
    Binding sitei27ATP; shared with dimeric partner3 Publications1
    Binding sitei139Substrate1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi190Magnesium; catalyticCurated1
    Binding sitei248ATP3 Publications1
    Metal bindingi250Potassium; via carbonyl oxygen1 Publication1
    Metal bindingi252Potassium; via carbonyl oxygen1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei256By similarity1
    Binding sitei256Substrate1
    Binding sitei280ATP; via carbonyl oxygen3 Publications1
    Binding sitei284ATP3 Publications1
    Metal bindingi286Potassium; via carbonyl oxygen1 Publication1
    Metal bindingi289Potassium; via carbonyl oxygen1 Publication1
    Metal bindingi291Potassium; via carbonyl oxygen1 Publication1
    Metal bindingi293Potassium; via carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi185 – 187ATP3 Publications3
    Nucleotide bindingi224 – 229ATP3 Publications6

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • 6-phosphofructokinase activity Source: EcoCyc
    • ATP binding Source: UniProtKB-KW
    • identical protein binding Source: IntAct
    • magnesium ion binding Source: EcoCyc
    • tagatose-6-phosphate kinase activity Source: EcoCyc
    Complete GO annotation on QuickGO ...

    GO - Biological processi

    • cellular response to DNA damage stimulus Source: EcoliWiki
    • glycolytic process Source: EcoCyc
    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionKinase, Transferase
    Biological processGlycolysis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:6PFK-2-MONOMER
    ECOL316407:JW5280-MONOMER
    MetaCyc:6PFK-2-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.1.11 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P06999

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00109;UER00182

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase isozyme 2 (EC:2.7.1.11)
    Short name:
    ATP-PFK 2
    Short name:
    Phosphofructokinase 2
    Alternative name(s):
    6-phosphofructokinase isozyme II
    Phosphohexokinase 2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:pfkB
    Ordered Locus Names:b1723, JW5280
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...    EcoGenei    		EG10700 pfkB

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation on QuickGO ...

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi190E → Q: Causes a 50-fold decrease in the kcat value and a 15-fold increment in the apparent KM for ATP. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000800831 – 309ATP-dependent 6-phosphofructokinase isozyme 2Add BLAST309

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P06999

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P06999

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P06999

    PRoteomics IDEntifications database

    More...    PRIDEi    		P06999

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...    SWISS-2DPAGEi    		P06999

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    5 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-6966085,EBI-6966085

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4263076, 25 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-10465N

    Molecular INTeraction database

    More...    MINTi    		P06999

    STRING: functional protein association networks

    More...    STRINGi    		511145.b1723

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1309
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P06999

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P06999

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni12 – 14Substrate binding3
    Regioni27 – 29Substrate binding3
    Regioni39 – 43Substrate binding5
    Regioni90 – 92Substrate binding3
    Regioni187 – 189Allosteric inhibitor ATP binding3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the carbohydrate kinase PfkB family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105DE4 Bacteria
    COG1105 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000265281

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P06999

    KEGG Orthology (KO)

    More...    KOi    		K16370

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P06999

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd01164 FruK_PfkB_like, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.1190.20, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR002173 Carboh/pur_kinase_PfkB_CS
    IPR011611 PfkB_dom
    IPR029056 Ribokinase-like
    IPR017583 Tagatose/fructose_Pkinase

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00294 PfkB, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000535 1PFK/6PFK/LacC, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53613 SSF53613, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR03168 1-PFK, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00583 PFKB_KINASES_1, 1 hit
    PS00584 PFKB_KINASES_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P06999-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVRIYTLTLA PSLDSATITP QIYPEGKLRC TAPVFEPGGG GINVARAIAH 
            60         70         80         90        100
    LGGSATAIFP AGGATGEHLV SLLADENVPV ATVEAKDWTR QNLHVHVEAS 
           110        120        130        140        150
    GEQYRFVMPG AALNEDEFRQ LEEQVLEIES GAILVISGSL PPGVKLEKLT 
           160        170        180        190        200
    QLISAAQKQG IRCIVDSSGE ALSAALAIGN IELVKPNQKE LSALVNRELT 
           210        220        230        240        250
    QPDDVRKAAQ EIVNSGKAKR VVVSLGPQGA LGVDSENCIQ VVPPPVKSQS 
           260        270        280        290        300
    TVGAGDSMVG AMTLKLAENA SLEEMVRFGV AAGSAATLNQ GTRLCSHDDT 

    QKIYAYLSR
    Length:309
    Mass (Da):32,456
    Last modified:November 1, 1997 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA93BEBE0D5801309
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26 – 38GKLRC…VFEPG → ENCAVPHRCSNP in AAA24321 (PubMed:6235149).CuratedAdd BLAST13
    Sequence conflicti26 – 38GKLRC…VFEPG → ENCAVPHRCSNP in AAA24320 (PubMed:6310120).CuratedAdd BLAST13
    Sequence conflicti155 – 171AAQKQ…SSGEA → LRKNKGSAASSTVLGQG in AAA24321 (PubMed:6235149).CuratedAdd BLAST17
    Sequence conflicti245 – 246PV → AL in AAA24321 (PubMed:6235149).Curated2
    Sequence conflicti257 – 258SM → RL in AAA24321 (PubMed:6235149).Curated2

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		K02500 Genomic DNA Translation: AAA24321.1
    U00096 Genomic DNA Translation: AAC74793.1
    AP009048 Genomic DNA Translation: BAA15500.2
    K00128 Genomic DNA Translation: AAA24320.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		C64931 KIECFB

    NCBI Reference Sequences

    More...    RefSeqi    		NP_416237.3, NC_000913.3
    WP_000251727.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC74793; AAC74793; b1723
    BAA15500; BAA15500; BAA15500

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		946230

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW5280
    eco:b1723

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.533

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		K02500 Genomic DNA Translation: AAA24321.1
    U00096 Genomic DNA Translation: AAC74793.1
    AP009048 Genomic DNA Translation: BAA15500.2
    K00128 Genomic DNA Translation: AAA24320.1
    PIRiC64931 KIECFB
    RefSeqiNP_416237.3, NC_000913.3
    WP_000251727.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3CQDX-ray1.98A/B1-309[»]
    3N1CX-ray2.00A/B/C/D1-309[»]
    3UMOX-ray1.70A/B1-309[»]
    3UMPX-ray1.85A/B1-309[»]
    3UQDX-ray2.14A/B/C/D1-309[»]
    3UQEX-ray2.20A/B1-309[»]
    SMRiP06999
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4263076, 25 interactors
    DIPiDIP-10465N
    MINTiP06999
    STRINGi511145.b1723

    2D gel databases

    SWISS-2DPAGEiP06999

    Proteomic databases

    EPDiP06999
    jPOSTiP06999
    PaxDbiP06999
    PRIDEiP06999

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74793; AAC74793; b1723
    BAA15500; BAA15500; BAA15500
    GeneIDi946230
    KEGGiecj:JW5280
    eco:b1723
    PATRICifig|1411691.4.peg.533

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB0694
    EcoGeneiEG10700 pfkB

    Phylogenomic databases

    eggNOGiENOG4105DE4 Bacteria
    COG1105 LUCA
    HOGENOMiHOG000265281
    InParanoidiP06999
    KOiK16370
    PhylomeDBiP06999

    Enzyme and pathway databases

    UniPathwayiUPA00109;UER00182
    BioCyciEcoCyc:6PFK-2-MONOMER
    ECOL316407:JW5280-MONOMER
    MetaCyc:6PFK-2-MONOMER
    BRENDAi2.7.1.11 2026
    SABIO-RKiP06999

    Miscellaneous databases

    EvolutionaryTraceiP06999

    Protein Ontology

    More...    PROi    		PR:P06999

    Family and domain databases

    CDDicd01164 FruK_PfkB_like, 1 hit
    Gene3Di3.40.1190.20, 1 hit
    InterProiView protein in InterPro
    IPR002173 Carboh/pur_kinase_PfkB_CS
    IPR011611 PfkB_dom
    IPR029056 Ribokinase-like
    IPR017583 Tagatose/fructose_Pkinase
    PfamiView protein in Pfam
    PF00294 PfkB, 1 hit
    PIRSFiPIRSF000535 1PFK/6PFK/LacC, 1 hit
    SUPFAMiSSF53613 SSF53613, 1 hit
    TIGRFAMsiTIGR03168 1-PFK, 1 hit
    PROSITEiView protein in PROSITE
    PS00583 PFKB_KINASES_1, 1 hit
    PS00584 PFKB_KINASES_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPFKB_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06999
    Secondary accession number(s): P78065, P78260
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: November 1, 1997
    Last modified: June 5, 2019
    This is version 163 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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