Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 88 (08 May 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

ATP-dependent 6-phosphofructokinase

Gene

PFK

Organism
Schistosoma mansoni (Blood fluke)
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.UniRule annotation1 Publication

<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+UniRule annotation

<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 activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation1 Publication

<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=3.5 mM for ATP1 Publication
  2. KM=0.8 mM for fructose 6-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.5-9.0.1 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.UniRule annotation
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Hexokinase
    2. Glucose-6-phosphate isomerase (Smp_022400)
    3. ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (Smp_043670.1), ATP-dependent 6-phosphofructokinase (Smp_043670.2), ATP-dependent 6-phosphofructokinase
    4. Fructose-bisphosphate aldolase (Smp_042160.1), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (Smp_042160.2)
    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 sitei27ATP; via amide nitrogenUniRule annotation1
    <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 bindingi121Magnesium; catalyticUniRule annotation1
    <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 sitei168Proton acceptorUniRule annotation1
    Binding sitei203Substrate; shared with dimeric partnerUniRule annotation1
    Binding sitei266SubstrateUniRule annotation1
    Binding sitei294Substrate; shared with dimeric partnerUniRule annotation1
    Binding sitei479Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
    Binding sitei575Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
    Binding sitei638Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
    Binding sitei664Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
    Binding sitei745Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

    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 bindingi90 – 91ATPUniRule annotation2
    Nucleotide bindingi120 – 123ATPUniRule annotation4

    <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

    GO - Biological processi

    <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 functionAllosteric enzyme, Kinase, Transferase
    Biological processGlycolysis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q27778

    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-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PhosphofructokinaseUniRule annotation
    Alternative name(s):
    PhosphohexokinaseUniRule annotation
    <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:PFK
    <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>OrganismiSchistosoma mansoni (Blood fluke)
    <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 identifieri6183 [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 lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma
    <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
    • UP000008854 <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: Unassembled WGS sequence

    <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

    Keywords - Cellular componenti

    Cytoplasm

    <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_00001120331 – 781ATP-dependent 6-phosphofructokinaseAdd BLAST781

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q27778

    <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

    Homotetramer.

    UniRule annotation

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    6183.Smp_043670.2

    <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

    3D structure databases

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

    More...
    SMRi
    Q27778

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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>Regioni1 – 394N-terminal catalytic PFK domain 1Add BLAST394
    Regioni166 – 168Substrate bindingUniRule annotation3
    Regioni210 – 212Substrate bindingUniRule annotation3
    Regioni300 – 303Substrate bindingUniRule annotation4
    Regioni395 – 409Interdomain linkerAdd BLAST15
    Regioni410 – 781C-terminal regulatory PFK domain 2Add BLAST372
    Regioni537 – 541Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
    Regioni582 – 584Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
    Regioni670 – 673Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation4

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2440 Eukaryota
    COG0205 LUCA

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_03184 Phosphofructokinase_I_E, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR009161 6-Pfructokinase_euk
    IPR022953 ATP_PFK
    IPR015912 Phosphofructokinase_CS
    IPR000023 Phosphofructokinase_dom
    IPR035966 PKF_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00365 PFK, 2 hits

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000533 ATP_PFK_euk, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00476 PHFRCTKINASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53784 SSF53784, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02478 6PF1K_euk, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00433 PHOSPHOFRUCTOKINASE, 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.

    Q27778-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MATWMEGKYV ARGQFTGECI AVLTSGGDAQ GMNAAVRAVV RMGIYCGCRV
    60 70 80 90 100
    FFIREGYQGL VDGGQNIQEA SWADVSGILQ LGGTKIGSAR CMDFRERYGR
    110 120 130 140 150
    LKAAENLVKN QITNLVVIGG DGSLTGANLF RAEWSSLLEE LVTSNKISAE
    160 170 180 190 200
    SAKQFHRLNI VGLVGSIDND FCGTDMTIGA DSALHRIIEA TDAISTTAHS
    210 220 230 240 250
    HQRCFILEVM GRHCGYLALV ASMACEADWV FIPEMPPTDD WREKLCHKLR
    260 270 280 290 300
    MNREHGQRVN IIMVAEGAID RACKPITCEI VKNLIVSELQ LDTRITVLGH
    310 320 330 340 350
    VQRGGSPSAF DRILGSRMGA EAVLALMDAD RDPNLPSCVI SLDGNQAVRV
    360 370 380 390 400
    PLVKCVDRTR QVAEAMKACD FDHAVELRGT SFMNNLATYI KLSKIEQPRQ
    410 420 430 440 450
    SVMSSENNLR IGIVNVGAPA CGINAVIRGF TRLGITKGYK VIGIHEGFSG
    460 470 480 490 500
    LVKGDASEIQ WADVRGWVGM GGSMLGTRRD TPNGLGIDKV AAKFKELKLS
    510 520 530 540 550
    GLLIIGGFEA YECMIELVEG REKYPELCIP MAMVPATISN NVPGTDFSLG
    560 570 580 590 600
    CDTALNEITS VLDKIKQSAL GTKRRVFVVE TMGGYCGYLA TMSALAGGAD
    610 620 630 640 650
    AAYIFEEPFT IDDLREDVVH LRAKIDDNVK RGLVLRADML INTITSEFIH
    660 670 680 690 700
    QLYAQEGQGI FDCRCNVLGH MQQGDRPSPF DRSLGTKFAS KAIDWLDEQI
    710 720 730 740 750
    NANIVQILQS IHQTFMLYIN WYCTSSDNLF KYSLELREHT DFVHRLPKEE
    760 770 780
    WWLSLRPLMR IMAKHDSLYE SESIMAGTDR K
    Length:781
    Mass (Da):86,060
    Last modified:November 1, 1996 - v1
    <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:iB2CDF20CAE926C38
    GO

    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
    L31531 mRNA Translation: AAA29911.1

    Genome annotation databases

    GeneDB pathogen genome database from Sanger Institute

    More...
    GeneDBi
    Smp_043670.1:pep
    Smp_043670.2:pep

    <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
    L31531 mRNA Translation: AAA29911.1

    3D structure databases

    SMRiQ27778
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi6183.Smp_043670.2

    Proteomic databases

    PRIDEiQ27778

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneDBiSmp_043670.1:pep
    Smp_043670.2:pep

    Phylogenomic databases

    eggNOGiKOG2440 Eukaryota
    COG0205 LUCA

    Enzyme and pathway databases

    UniPathwayiUPA00109;UER00182
    SABIO-RKiQ27778

    Family and domain databases

    HAMAPiMF_03184 Phosphofructokinase_I_E, 1 hit
    InterProiView protein in InterPro
    IPR009161 6-Pfructokinase_euk
    IPR022953 ATP_PFK
    IPR015912 Phosphofructokinase_CS
    IPR000023 Phosphofructokinase_dom
    IPR035966 PKF_sf
    PfamiView protein in Pfam
    PF00365 PFK, 2 hits
    PIRSFiPIRSF000533 ATP_PFK_euk, 1 hit
    PRINTSiPR00476 PHFRCTKINASE
    SUPFAMiSSF53784 SSF53784, 2 hits
    TIGRFAMsiTIGR02478 6PF1K_euk, 1 hit
    PROSITEiView protein in PROSITE
    PS00433 PHOSPHOFRUCTOKINASE, 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 nameiPFKA_SCHMA
    <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: Q27778
    <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: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: May 8, 2019
    This is version 88 of the entry and version 1 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)

    <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

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again