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Entry version 184 (31 Jul 2019)
Sequence version 1 (01 Aug 1990)
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Protein

ATP-dependent 6-phosphofructokinase subunit alpha

Gene

PFK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 annotation8 Publications

Miscellaneous

Present with 89800 molecules/cell in log phase SD medium.1 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 annotationBy similarity

<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 annotation3 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=0.24 mM for ATP (without effector)1 Publication
  2. KM=0.3 mM for ATP (with 1 mM AMP)1 Publication
  3. KM=0.31 mM for ATP (with 20 µM fructose 2,6-bisphosphate)1 Publication
  4. KM=1.65 mM for fructose 6-phosphate (without effector)1 Publication
  5. KM=0.51 mM for fructose 6-phosphate (with 1 mM AMP)1 Publication
  6. KM=0.11 mM for fructose 6-phosphate (with 20 µM fructose 2,6-bisphosphate)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. Putative hexokinase YLR446W (YLR446W), Hexokinase-1 (HXK1), Glucokinase-1 (GLK1), Hexokinase-2 (HXK2), Putative glucokinase-2 (EMI2)
    2. Glucose-6-phosphate isomerase (PGI1)
    3. ATP-dependent 6-phosphofructokinase subunit beta (PFK2), ATP-dependent 6-phosphofructokinase subunit alpha (PFK1)
    4. Fructose-bisphosphate aldolase (FBA1)
    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 sitei215ATP; via amide nitrogenUniRule annotationBy similarity1
    <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 bindingi309Magnesium; catalyticUniRule annotationBy similarity1
    <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 sitei356Proton acceptorUniRule annotationBy similarity1
    Binding sitei391Substrate; shared with subunit beta1 Publication1
    Binding sitei455Substrate1 Publication1
    Binding sitei482Substrate; shared with subunit beta1 Publication1
    Binding sitei665Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 Publication1
    Binding sitei760Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation1 Publication1
    Binding sitei827Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 Publication1
    Binding sitei853Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation1 Publication1
    Binding sitei952Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 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 bindingi278 – 279ATPUniRule annotationBy similarity2
    Nucleotide bindingi308 – 311ATPUniRule annotationBy similarity4

    <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

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YGR240C-MONOMER
    YEAST:YGR240C-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-6798695 Neutrophil degranulation
    R-SCE-70171 Glycolysis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P16861

    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 subunit alphaUniRule annotation (EC:2.7.1.11UniRule annotation)
    Alternative name(s):
    ATP-dependent 6-phosphofructokinaseUniRule annotation
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    Phosphofructokinase 1UniRule annotation
    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:PFK1
    Ordered Locus Names:YGR240C
    ORF Names:G8599
    <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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <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
    • UP000002311 <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 VII

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YGR240C

    Saccharomyces Genome Database

    More...
    SGDi
    S000003472 PFK1

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    <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>Mutagenesisi309D → T: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. 1 Publication1
    Mutagenesisi356D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. 1 Publication1
    Mutagenesisi447R → S: Reduces maximal activity of the holoenzyme by less than 25%. 1 Publication1
    Mutagenesisi488H → S: Increases the KM for fructose 6-phosphate 20 fold. 1 Publication1
    Mutagenesisi724S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-718' in subunit beta. 1 Publication1
    Mutagenesisi728P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. 1 Publication1
    Mutagenesisi859H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-853' in subunit beta. 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_00001120451 – 987ATP-dependent 6-phosphofructokinase subunit alphaAdd BLAST987

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3PhosphoserineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei166PhosphoserineCombined sources1
    Modified residuei179PhosphoserineCombined sources1
    Modified residuei185PhosphoserineCombined sources1
    Modified residuei189PhosphoserineCombined sources1
    Modified residuei192PhosphoserineCombined sources1
    Modified residuei217PhosphoserineCombined sources1
    Modified residuei450PhosphothreonineCombined sources1
    Cross-linki625Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P16861

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

    More...
    PaxDbi
    P16861

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P16861

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P16861

    <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

    Heterooctamer of 4 alpha and 4 beta chains.

    UniRule annotation3 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
    PFK2P168625EBI-9428,EBI-9435

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    33492, 264 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-554 6-phosphofructokinase complex

    Database of interacting proteins

    More...
    DIPi
    DIP-1505N

    Protein interaction database and analysis system

    More...
    IntActi
    P16861, 72 interactors

    Molecular INTeraction database

    More...
    MINTi
    P16861

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YGR240C

    <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

    1987
    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
    P16861

    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 – 580N-terminal catalytic PFK domain 1UniRule annotation1 PublicationAdd BLAST580
    Regioni354 – 356Substrate bindingUniRule annotation1 Publication3
    Regioni398 – 400Substrate bindingUniRule annotation1 Publication3
    Regioni488 – 491Substrate bindingUniRule annotation1 Publication4
    Regioni581 – 594Interdomain linkerUniRule annotation1 PublicationAdd BLAST14
    Regioni595 – 987C-terminal regulatory PFK domain 2UniRule annotation1 PublicationAdd BLAST393
    Regioni722 – 726Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation1 Publication5
    Regioni767 – 769Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation1 Publication3
    Regioni859 – 862Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation1 Publication4

    <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

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000200154

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P16861

    KEGG Orthology (KO)

    More...
    KOi
    K00850

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GCKAYFI

    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
    IPR040712 Pfk_N
    IPR015912 Phosphofructokinase_CS
    IPR000023 Phosphofructokinase_dom
    IPR035966 PKF_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00365 PFK, 2 hits
    PF18468 Pfk_N, 1 hit

    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, 2 hits

    <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.

    P16861-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQSQDSCYGV AFRSIITNDE ALFKKTIHFY HTLGFATVKD FNKFKHGENS
    60 70 80 90 100
    LLSSGTSQDS LREVWLESFK LSEVDASGFR IPQQEATNKA QSQGALLKIR
    110 120 130 140 150
    LVMSAPIDET FDTNETATIT YFSTDLNKIV EKFPKQAEKL SDTLVFLKDP
    160 170 180 190 200
    MGNNITFSGL ANATDSAPTS KDAFLEATSE DEIISRASSD ASDLLRQTLG
    210 220 230 240 250
    SSQKKKKIAV MTSGGDSPGM NAAVRAVVRT GIHFGCDVFA VYEGYEGLLR
    260 270 280 290 300
    GGKYLKKMAW EDVRGWLSEG GTLIGTARSM EFRKREGRRQ AAGNLISQGI
    310 320 330 340 350
    DALVVCGGDG SLTGADLFRH EWPSLVDELV AEGRFTKEEV APYKNLSIVG
    360 370 380 390 400
    LVGSIDNDMS GTDSTIGAYS ALERICEMVD YIDATAKSHS RAFVVEVMGR
    410 420 430 440 450
    HCGWLALMAG IATGADYIFI PERAVPHGKW QDELKEVCQR HRSKGRRNNT
    460 470 480 490 500
    IIVAEGALDD QLNPVTANDV KDALIELGLD TKVTILGHVQ RGGTAVAHDR
    510 520 530 540 550
    WLATLQGVDA VKAVLEFTPE TPSPLIGILE NKIIRMPLVE SVKLTKSVAT
    560 570 580 590 600
    AIENKDFDKA ISLRDTEFIE LYENFLSTTV KDDGSELLPV SDRLNIGIVH
    610 620 630 640 650
    VGAPSAALNA ATRAATLYCL SHGHKPYAIM NGFSGLIQTG EVKELSWIDV
    660 670 680 690 700
    ENWHNLGGSE IGTNRSVASE DLGTIAYYFQ KNKLDGLIIL GGFEGFRSLK
    710 720 730 740 750
    QLRDGRTQHP IFNIPMCLIP ATVSNNVPGT EYSLGVDTCL NALVNYTDDI
    760 770 780 790 800
    KQSASATRRR VFVCEVQGGH SGYIASFTGL ITGAVSVYTP EKKIDLASIR
    810 820 830 840 850
    EDITLLKENF RHDKGENRNG KLLVRNEQAS SVYSTQLLAD IISEASKGKF
    860 870 880 890 900
    GVRTAIPGHV QQGGVPSSKD RVTASRFAVK CIKFIEQWNK KNEASPNTDA
    910 920 930 940 950
    KVLRFKFDTH GEKVPTVEHE DDSAAVICVN GSHVSFKPIA NLWENETNVE
    960 970 980
    LRKGFEVHWA EYNKIGDILS GRLKLRAEVA ALAAENK
    Length:987
    Mass (Da):107,970
    Last modified:August 1, 1990 - 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:i995B3DF7C7781B29
    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
    M26943 Genomic DNA Translation: AAA34859.1
    Z73025 Genomic DNA Translation: CAA97268.1
    X87941 Genomic DNA Translation: CAA61193.1
    BK006941 Genomic DNA Translation: DAA08331.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JQ0016

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_011756.1, NM_001181369.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YGR240C_mRNA; YGR240C_mRNA; YGR240C

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    853155

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YGR240C

    <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
    M26943 Genomic DNA Translation: AAA34859.1
    Z73025 Genomic DNA Translation: CAA97268.1
    X87941 Genomic DNA Translation: CAA61193.1
    BK006941 Genomic DNA Translation: DAA08331.1
    PIRiJQ0016
    RefSeqiNP_011756.1, NM_001181369.1

    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
    3O8OX-ray2.90A/C/E/G201-987[»]
    SMRiP16861
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi33492, 264 interactors
    ComplexPortaliCPX-554 6-phosphofructokinase complex
    DIPiDIP-1505N
    IntActiP16861, 72 interactors
    MINTiP16861
    STRINGi4932.YGR240C

    PTM databases

    iPTMnetiP16861

    Proteomic databases

    MaxQBiP16861
    PaxDbiP16861
    PRIDEiP16861

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR240C_mRNA; YGR240C_mRNA; YGR240C
    GeneIDi853155
    KEGGisce:YGR240C

    Organism-specific databases

    EuPathDBiFungiDB:YGR240C
    SGDiS000003472 PFK1

    Phylogenomic databases

    HOGENOMiHOG000200154
    InParanoidiP16861
    KOiK00850
    OMAiGCKAYFI

    Enzyme and pathway databases

    UniPathwayiUPA00109;UER00182
    BioCyciMetaCyc:YGR240C-MONOMER
    YEAST:YGR240C-MONOMER
    ReactomeiR-SCE-6798695 Neutrophil degranulation
    R-SCE-70171 Glycolysis
    SABIO-RKiP16861

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P16861

    Family and domain databases

    HAMAPiMF_03184 Phosphofructokinase_I_E, 1 hit
    InterProiView protein in InterPro
    IPR009161 6-Pfructokinase_euk
    IPR022953 ATP_PFK
    IPR040712 Pfk_N
    IPR015912 Phosphofructokinase_CS
    IPR000023 Phosphofructokinase_dom
    IPR035966 PKF_sf
    PfamiView protein in Pfam
    PF00365 PFK, 2 hits
    PF18468 Pfk_N, 1 hit
    PIRSFiPIRSF000533 ATP_PFK_euk, 1 hit
    PRINTSiPR00476 PHFRCTKINASE
    SUPFAMiSSF53784 SSF53784, 2 hits
    TIGRFAMsiTIGR02478 6PF1K_euk, 1 hit
    PROSITEiView protein in PROSITE
    PS00433 PHOSPHOFRUCTOKINASE, 2 hits

    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 nameiPFKA1_YEAST
    <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: P16861
    Secondary accession number(s): D6VV20
    <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: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: July 31, 2019
    This is version 184 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)
    Annotation programFungal 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, Direct protein sequencing, 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. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
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