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Protein

Pyruvate kinase 1

Gene

CDC19

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

Miscellaneous

Present with 291000 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

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ 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

The activity is regulated by glucose levels. Activated by fructose-1,6-bisphosphate.

<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=0.31 mM for phosphoenolpyruvate (with magnesium as divalent cation)1 Publication
  2. KM=0.021 mM for phosphoenolpyruvate (with manganese as divalent cation)1 Publication
  3. KM=1.10 mM for ADP (with magnesium as divalent cation)1 Publication
  4. KM=0.24 mM for ADP (with manganese as divalent cation)1 Publication

    pH dependencei

    Optimum pH is 6.0.1 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 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Glyceraldehyde-3-phosphate dehydrogenase 2 (TDH2), Glyceraldehyde-3-phosphate dehydrogenase 3 (TDH3), Glyceraldehyde-3-phosphate dehydrogenase 1 (TDH1)
    2. Phosphoglycerate kinase (PGK1)
    3. Phosphoglycerate mutase 2 (GPM2), Phosphoglycerate mutase 1 (GPM1), Phosphoglycerate mutase 3 (GPM3)
    4. Enolase 2 (ENO2), Enolase 1 (ENO1), Enolase-related protein 1 (ERR1), Enolase-related protein 2 (ERR2), Enolase-related protein 3 (ERR3)
    5. Pyruvate kinase 1 (CDC19), Pyruvate kinase 2 (PYK2)
    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 pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei49SubstrateCombined sources1 Publication1
    <p>This subsection of the ‘Function’ 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 bindingi51PotassiumCombined sources1 Publication1
    Metal bindingi53PotassiumCombined sources1 Publication1
    Metal bindingi84PotassiumCombined sources1 Publication1
    Metal bindingi85Potassium; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei240Substrate; via amide nitrogenCombined sources1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei240Transition state stabilizer1 Publication1
    Metal bindingi242ManganeseCombined sources1 Publication1
    Binding sitei265Substrate; via amide nitrogenCombined sources1 Publication1
    Metal bindingi266ManganeseCombined sources1 Publication1
    Binding sitei266Substrate; via amide nitrogenCombined sources1 Publication1
    Binding sitei298SubstrateCombined sources1 Publication1
    Binding sitei337ADPSequence analysis1
    Binding sitei452Allosteric activatorCombined sources1 Publication1
    Binding sitei459Allosteric activatorCombined sources1 Publication1
    Binding sitei484Allosteric activator; via amide nitrogenCombined sources1 Publication1

    <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

    • cellular response to insulin stimulus Source: GO_Central
    • glycolytic process Source: SGD
    • pyruvate metabolic process Source: SGD

    <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, Potassium, Pyruvate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:YAL038W-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
    P00549

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

    More...
    UniPathwayi
    UPA00109;UER00188

    Protein family/group databases

    MoonProt database of moonlighting proteins

    More...
    MoonProti
    P00549

    <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:
    Pyruvate kinase 1 (EC:2.7.1.401 Publication)
    Short name:
    PK 1
    Alternative name(s):
    cell division cycle protein 19
    <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:CDC19
    Synonyms:PYK1
    Ordered Locus Names:YAL038W
    <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 I

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000000036 CDC19

    <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

    <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>Mutagenesisi240K → M: Reduces activity 1000-fold. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <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_00001121212 – 500Pyruvate kinase 1Add BLAST499

    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 residuei2N-acetylserineCombined sources1
    Modified residuei9PhosphoserineCombined sources1
    Modified residuei16PhosphoserineCombined sources1
    Modified residuei31PhosphothreonineCombined sources1
    Modified residuei70PhosphoserineCombined sources1
    Modified residuei184PhosphothreonineCombined 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-linki204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei213PhosphoserineCombined sources1
    Cross-linki255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei316PhosphoserineCombined sources1
    Cross-linki446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei450PhosphoserineCombined sources1
    Modified residuei478PhosphothreonineCombined sources1

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P00549

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

    More...
    PaxDbi
    P00549

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P00549

    Consortium for Top Down Proteomics

    More...
    TopDownProteomicsi
    P00549

    2D gel databases

    2-DE database at Universidad Complutense de Madrid

    More...
    COMPLUYEAST-2DPAGEi
    P00549

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P00549

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P00549

    <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.

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    31727, 278 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-4124N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    P00549

    Protein interaction database and analysis system

    More...
    IntActi
    P00549, 185 interactors

    Molecular INTeraction database

    More...
    MINTi
    P00549

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YAL038W

    <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

    1500
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P00549

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

    More...
    SMRi
    P00549

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P00549

    <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>Regioni402 – 407Allosteric activator bindingCombined sources1 Publication6

    <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 pyruvate kinase family.Curated

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000008859

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000021559

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P00549

    KEGG Orthology (KO)

    More...
    KOi
    K00873

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    KHEAIEQ

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG092C1RXZ

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00288 Pyruvate_Kinase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.40.33.10, 1 hit
    3.40.1380.20, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001697 Pyr_Knase
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR011037 Pyrv_Knase-like_insert_dom_sf
    IPR018209 Pyrv_Knase_AS
    IPR015793 Pyrv_Knase_brl
    IPR015795 Pyrv_Knase_C
    IPR036918 Pyrv_Knase_C_sf
    IPR015806 Pyrv_Knase_insert_dom_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11817 PTHR11817, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00224 PK, 1 hit
    PF02887 PK_C, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01050 PYRUVTKNASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50800 SSF50800, 1 hit
    SSF51621 SSF51621, 1 hit
    SSF52935 SSF52935, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01064 pyruv_kin, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00110 PYRUVATE_KINASE, 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>.<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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P00549-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSRLERLTSL NVVAGSDLRR TSIIGTIGPK TNNPETLVAL RKAGLNIVRM
    60 70 80 90 100
    NFSHGSYEYH KSVIDNARKS EELYPGRPLA IALDTKGPEI RTGTTTNDVD
    110 120 130 140 150
    YPIPPNHEMI FTTDDKYAKA CDDKIMYVDY KNITKVISAG RIIYVDDGVL
    160 170 180 190 200
    SFQVLEVVDD KTLKVKALNA GKICSHKGVN LPGTDVDLPA LSEKDKEDLR
    210 220 230 240 250
    FGVKNGVHMV FASFIRTAND VLTIREVLGE QGKDVKIIVK IENQQGVNNF
    260 270 280 290 300
    DEILKVTDGV MVARGDLGIE IPAPEVLAVQ KKLIAKSNLA GKPVICATQM
    310 320 330 340 350
    LESMTYNPRP TRAEVSDVGN AILDGADCVM LSGETAKGNY PINAVTTMAE
    360 370 380 390 400
    TAVIAEQAIA YLPNYDDMRN CTPKPTSTTE TVAASAVAAV FEQKAKAIIV
    410 420 430 440 450
    LSTSGTTPRL VSKYRPNCPI ILVTRCPRAA RFSHLYRGVF PFVFEKEPVS
    460 470 480 490 500
    DWTDDVEARI NFGIEKAKEF GILKKGDTYV SIQGFKAGAG HSNTLQVSTV
    Length:500
    Mass (Da):54,545
    Last modified:July 1, 1989 - 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:i78D753FC410C5820
    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 conflicti382 – 386VAASA → SLPR in CAA24631 (PubMed:2653861).Curated5

    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
    V01321 Genomic DNA Translation: CAA24631.1
    X14400 Genomic DNA Translation: CAA32573.1
    AY949862 Genomic DNA Translation: AAY27264.1
    AY949863 Genomic DNA Translation: AAY27265.1
    AY949864 Genomic DNA Translation: AAY27266.1
    AY949865 Genomic DNA Translation: AAY27267.1
    AY949866 Genomic DNA Translation: AAY27268.1
    AY949867 Genomic DNA Translation: AAY27269.1
    AY949868 Genomic DNA Translation: AAY27270.1
    AY949869 Genomic DNA Translation: AAY27271.1
    AY949870 Genomic DNA Translation: AAY27272.1
    AY949871 Genomic DNA Translation: AAY27273.1
    AY949872 Genomic DNA Translation: AAY27274.1
    AY949873 Genomic DNA Translation: AAY27275.1
    AY949874 Genomic DNA Translation: AAY27276.1
    AY949875 Genomic DNA Translation: AAY27277.1
    AY949876 Genomic DNA Translation: AAY27278.1
    AY949877 Genomic DNA Translation: AAY27279.1
    AY949878 Genomic DNA Translation: AAY27280.1
    AY949879 Genomic DNA Translation: AAY27281.1
    AY949880 Genomic DNA Translation: AAY27282.1
    AY949881 Genomic DNA Translation: AAY27283.1
    AY949882 Genomic DNA Translation: AAY27284.1
    AY949883 Genomic DNA Translation: AAY27285.1
    AY949884 Genomic DNA Translation: AAY27286.1
    AY949885 Genomic DNA Translation: AAY27287.1
    AY949886 Genomic DNA Translation: AAY27288.1
    AY949887 Genomic DNA Translation: AAY27289.1
    AY949888 Genomic DNA Translation: AAY27290.1
    AY949889 Genomic DNA Translation: AAY27291.1
    AY949890 Genomic DNA Translation: AAY27292.1
    U12980 Genomic DNA Translation: AAC04993.1
    AY693107 Genomic DNA Translation: AAT93126.1
    BK006935 Genomic DNA Translation: DAA06948.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S05764 KIBYP

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_009362.1, NM_001178183.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YAL038W_mRNA; YAL038W_mRNA; YAL038W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    851193

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YAL038W

    <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
    V01321 Genomic DNA Translation: CAA24631.1
    X14400 Genomic DNA Translation: CAA32573.1
    AY949862 Genomic DNA Translation: AAY27264.1
    AY949863 Genomic DNA Translation: AAY27265.1
    AY949864 Genomic DNA Translation: AAY27266.1
    AY949865 Genomic DNA Translation: AAY27267.1
    AY949866 Genomic DNA Translation: AAY27268.1
    AY949867 Genomic DNA Translation: AAY27269.1
    AY949868 Genomic DNA Translation: AAY27270.1
    AY949869 Genomic DNA Translation: AAY27271.1
    AY949870 Genomic DNA Translation: AAY27272.1
    AY949871 Genomic DNA Translation: AAY27273.1
    AY949872 Genomic DNA Translation: AAY27274.1
    AY949873 Genomic DNA Translation: AAY27275.1
    AY949874 Genomic DNA Translation: AAY27276.1
    AY949875 Genomic DNA Translation: AAY27277.1
    AY949876 Genomic DNA Translation: AAY27278.1
    AY949877 Genomic DNA Translation: AAY27279.1
    AY949878 Genomic DNA Translation: AAY27280.1
    AY949879 Genomic DNA Translation: AAY27281.1
    AY949880 Genomic DNA Translation: AAY27282.1
    AY949881 Genomic DNA Translation: AAY27283.1
    AY949882 Genomic DNA Translation: AAY27284.1
    AY949883 Genomic DNA Translation: AAY27285.1
    AY949884 Genomic DNA Translation: AAY27286.1
    AY949885 Genomic DNA Translation: AAY27287.1
    AY949886 Genomic DNA Translation: AAY27288.1
    AY949887 Genomic DNA Translation: AAY27289.1
    AY949888 Genomic DNA Translation: AAY27290.1
    AY949889 Genomic DNA Translation: AAY27291.1
    AY949890 Genomic DNA Translation: AAY27292.1
    U12980 Genomic DNA Translation: AAC04993.1
    AY693107 Genomic DNA Translation: AAT93126.1
    BK006935 Genomic DNA Translation: DAA06948.1
    PIRiS05764 KIBYP
    RefSeqiNP_009362.1, NM_001178183.1

    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
    1A3WX-ray3.00A/B1-500[»]
    1A3XX-ray3.00A/B1-500[»]
    ProteinModelPortaliP00549
    SMRiP00549
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31727, 278 interactors
    DIPiDIP-4124N
    ELMiP00549
    IntActiP00549, 185 interactors
    MINTiP00549
    STRINGi4932.YAL038W

    Protein family/group databases

    MoonProtiP00549

    PTM databases

    CarbonylDBiP00549
    iPTMnetiP00549

    2D gel databases

    COMPLUYEAST-2DPAGEiP00549

    Proteomic databases

    MaxQBiP00549
    PaxDbiP00549
    PRIDEiP00549
    TopDownProteomicsiP00549

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYAL038W_mRNA; YAL038W_mRNA; YAL038W
    GeneIDi851193
    KEGGisce:YAL038W

    Organism-specific databases

    SGDiS000000036 CDC19

    Phylogenomic databases

    GeneTreeiENSGT00390000008859
    HOGENOMiHOG000021559
    InParanoidiP00549
    KOiK00873
    OMAiKHEAIEQ
    OrthoDBiEOG092C1RXZ

    Enzyme and pathway databases

    UniPathwayi
    UPA00109;UER00188

    BioCyciYEAST:YAL038W-MONOMER
    ReactomeiR-SCE-6798695 Neutrophil degranulation
    R-SCE-70171 Glycolysis
    SABIO-RKiP00549

    Miscellaneous databases

    EvolutionaryTraceiP00549

    Protein Ontology

    More...
    PROi
    PR:P00549

    Family and domain databases

    CDDicd00288 Pyruvate_Kinase, 1 hit
    Gene3Di2.40.33.10, 1 hit
    3.40.1380.20, 1 hit
    InterProiView protein in InterPro
    IPR001697 Pyr_Knase
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR011037 Pyrv_Knase-like_insert_dom_sf
    IPR018209 Pyrv_Knase_AS
    IPR015793 Pyrv_Knase_brl
    IPR015795 Pyrv_Knase_C
    IPR036918 Pyrv_Knase_C_sf
    IPR015806 Pyrv_Knase_insert_dom_sf
    PANTHERiPTHR11817 PTHR11817, 1 hit
    PfamiView protein in Pfam
    PF00224 PK, 1 hit
    PF02887 PK_C, 1 hit
    PRINTSiPR01050 PYRUVTKNASE
    SUPFAMiSSF50800 SSF50800, 1 hit
    SSF51621 SSF51621, 1 hit
    SSF52935 SSF52935, 1 hit
    TIGRFAMsiTIGR01064 pyruv_kin, 1 hit
    PROSITEiView protein in PROSITE
    PS00110 PYRUVATE_KINASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiKPYK1_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: P00549
    Secondary accession number(s): D6VPH8, Q2VQG5
    <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 21, 1986
    Last sequence update: July 1, 1989
    Last modified: December 5, 2018
    This is version 198 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 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, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome I
      Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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