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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-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 Publication
  • K+1 Publication

Enzyme regulationi

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

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

    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 1 (TDH1), Glyceraldehyde-3-phosphate dehydrogenase 2 (TDH2), Glyceraldehyde-3-phosphate dehydrogenase 3 (TDH3)
    2. Phosphoglycerate kinase (PGK1)
    3. Phosphoglycerate mutase 2 (GPM2), Phosphoglycerate mutase 3 (GPM3), Phosphoglycerate mutase 1 (GPM1)
    4. Enolase 2 (ENO2), Enolase-related protein 2 (ERR2), Enolase-related protein 3 (ERR3), Enolase-related protein 1 (ERR1), Enolase 1 (ENO1)
    5. Pyruvate kinase 2 (PYK2), Pyruvate kinase 1 (CDC19)
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491SubstrateCombined sources1 Publication
    Metal bindingi51 – 511PotassiumCombined sources1 Publication
    Metal bindingi53 – 531PotassiumCombined sources1 Publication
    Metal bindingi84 – 841PotassiumCombined sources1 Publication
    Metal bindingi85 – 851Potassium; via carbonyl oxygenCombined sources1 Publication
    Binding sitei240 – 2401Substrate; via amide nitrogenCombined sources1 Publication
    Sitei240 – 2401Transition state stabilizer1 Publication
    Metal bindingi242 – 2421ManganeseCombined sources1 Publication
    Binding sitei265 – 2651Substrate; via amide nitrogenCombined sources1 Publication
    Metal bindingi266 – 2661ManganeseCombined sources1 Publication
    Binding sitei266 – 2661Substrate; via amide nitrogenCombined sources1 Publication
    Binding sitei298 – 2981SubstrateCombined sources1 Publication
    Binding sitei337 – 3371ADPSequence analysis
    Binding sitei452 – 4521Allosteric activatorCombined sources1 Publication
    Binding sitei459 – 4591Allosteric activatorCombined sources1 Publication
    Binding sitei484 – 4841Allosteric activator; via amide nitrogenCombined sources1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • glycolytic process Source: SGD
    • pyruvate metabolic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

    Enzyme and pathway databases

    BioCyciYEAST:YAL038W-MONOMER.
    ReactomeiR-SCE-70171. Glycolysis.
    SABIO-RKP00549.
    UniPathwayiUPA00109; UER00188.

    Names & Taxonomyi

    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
    Gene namesi
    Name:CDC19
    Synonyms:PYK1
    Ordered Locus Names:YAL038W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome I

    Organism-specific databases

    EuPathDBiFungiDB:YAL038W.
    SGDiS000000036. CDC19.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: SGD
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi240 – 2401K → M: Reduces activity 1000-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 500499Pyruvate kinase 1PRO_0000112121Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineCombined sources
    Modified residuei9 – 91PhosphoserineCombined sources
    Modified residuei16 – 161PhosphoserineCombined sources
    Modified residuei31 – 311PhosphothreonineCombined sources
    Modified residuei70 – 701PhosphoserineCombined sources
    Modified residuei184 – 1841PhosphothreonineCombined sources
    Cross-linki204 – 204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei213 – 2131PhosphoserineCombined sources
    Cross-linki255 – 255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei316 – 3161PhosphoserineCombined sources
    Cross-linki446 – 446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei450 – 4501PhosphoserineCombined sources
    Modified residuei478 – 4781PhosphothreonineCombined sources

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP00549.
    TopDownProteomicsiP00549.

    2D gel databases

    COMPLUYEAST-2DPAGEP00549.

    PTM databases

    iPTMnetiP00549.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi31727. 152 interactions.
    DIPiDIP-4124N.
    IntActiP00549. 184 interactions.
    MINTiMINT-565419.

    Structurei

    Secondary structure

    1
    500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 86Combined sources
    Beta strandi21 – 266Combined sources
    Helixi29 – 313Combined sources
    Helixi34 – 4310Combined sources
    Beta strandi47 – 493Combined sources
    Helixi57 – 7317Combined sources
    Beta strandi82 – 843Combined sources
    Beta strandi96 – 994Combined sources
    Beta strandi108 – 1125Combined sources
    Turni116 – 1205Combined sources
    Beta strandi126 – 1294Combined sources
    Helixi133 – 1364Combined sources
    Beta strandi142 – 1454Combined sources
    Turni146 – 1494Combined sources
    Beta strandi150 – 1534Combined sources
    Turni159 – 1613Combined sources
    Beta strandi163 – 1675Combined sources
    Beta strandi178 – 1803Combined sources
    Helixi193 – 20513Combined sources
    Beta strandi208 – 2125Combined sources
    Helixi218 – 23215Combined sources
    Beta strandi235 – 2417Combined sources
    Helixi245 – 2484Combined sources
    Helixi250 – 2567Combined sources
    Beta strandi260 – 2623Combined sources
    Helixi264 – 2707Combined sources
    Helixi273 – 2753Combined sources
    Helixi276 – 29015Combined sources
    Beta strandi294 – 2963Combined sources
    Helixi302 – 3054Combined sources
    Helixi312 – 32413Combined sources
    Beta strandi327 – 3293Combined sources
    Turni333 – 3375Combined sources
    Helixi341 – 35515Combined sources
    Beta strandi357 – 3593Combined sources
    Helixi361 – 3688Combined sources
    Helixi378 – 39316Combined sources
    Beta strandi398 – 4014Combined sources
    Beta strandi403 – 4053Combined sources
    Helixi406 – 4138Combined sources
    Beta strandi420 – 4256Combined sources
    Helixi429 – 4324Combined sources
    Helixi433 – 4353Combined sources
    Beta strandi439 – 4435Combined sources
    Turni452 – 4543Combined sources
    Helixi455 – 46915Combined sources
    Beta strandi478 – 4836Combined sources
    Turni487 – 4893Combined sources
    Beta strandi494 – 4996Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A3WX-ray3.00A/B1-500[»]
    1A3XX-ray3.00A/B1-500[»]
    ProteinModelPortaliP00549.
    SMRiP00549. Positions 2-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00549.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni402 – 4076Allosteric activator bindingCombined sources1 Publication

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000008859.
    HOGENOMiHOG000021559.
    InParanoidiP00549.
    KOiK00873.
    OMAiPENDHEY.
    OrthoDBiEOG092C1RXZ.

    Family and domain databases

    Gene3Di2.40.33.10. 1 hit.
    3.20.20.60. 2 hits.
    3.40.1380.20. 1 hit.
    InterProiIPR001697. Pyr_Knase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    IPR011037. Pyrv_Knase-like_insert_dom.
    IPR015794. Pyrv_Knase_a/b.
    IPR018209. Pyrv_Knase_AS.
    IPR015793. Pyrv_Knase_brl.
    IPR015795. Pyrv_Knase_C.
    IPR015806. Pyrv_Knase_insert_dom.
    [Graphical view]
    PANTHERiPTHR11817. PTHR11817. 1 hit.
    PfamiPF00224. PK. 1 hit.
    PF02887. PK_C. 1 hit.
    [Graphical view]
    PRINTSiPR01050. PYRUVTKNASE.
    SUPFAMiSSF50800. SSF50800. 1 hit.
    SSF51621. SSF51621. 2 hits.
    SSF52935. SSF52935. 1 hit.
    TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
    PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    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
    Checksum:i78D753FC410C5820
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti382 – 3865VAASA → SLPR in CAA24631 (PubMed:2653861).Curated

    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.

    Genome annotation databases

    EnsemblFungiiYAL038W; YAL038W; YAL038W.
    GeneIDi851193.
    KEGGisce:YAL038W.

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A3WX-ray3.00A/B1-500[»]
    1A3XX-ray3.00A/B1-500[»]
    ProteinModelPortaliP00549.
    SMRiP00549. Positions 2-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31727. 152 interactions.
    DIPiDIP-4124N.
    IntActiP00549. 184 interactions.
    MINTiMINT-565419.

    PTM databases

    iPTMnetiP00549.

    2D gel databases

    COMPLUYEAST-2DPAGEP00549.

    Proteomic databases

    MaxQBiP00549.
    TopDownProteomicsiP00549.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYAL038W; YAL038W; YAL038W.
    GeneIDi851193.
    KEGGisce:YAL038W.

    Organism-specific databases

    EuPathDBiFungiDB:YAL038W.
    SGDiS000000036. CDC19.

    Phylogenomic databases

    GeneTreeiENSGT00390000008859.
    HOGENOMiHOG000021559.
    InParanoidiP00549.
    KOiK00873.
    OMAiPENDHEY.
    OrthoDBiEOG092C1RXZ.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00188.
    BioCyciYEAST:YAL038W-MONOMER.
    ReactomeiR-SCE-70171. Glycolysis.
    SABIO-RKP00549.

    Miscellaneous databases

    EvolutionaryTraceiP00549.
    PROiP00549.

    Family and domain databases

    Gene3Di2.40.33.10. 1 hit.
    3.20.20.60. 2 hits.
    3.40.1380.20. 1 hit.
    InterProiIPR001697. Pyr_Knase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    IPR011037. Pyrv_Knase-like_insert_dom.
    IPR015794. Pyrv_Knase_a/b.
    IPR018209. Pyrv_Knase_AS.
    IPR015793. Pyrv_Knase_brl.
    IPR015795. Pyrv_Knase_C.
    IPR015806. Pyrv_Knase_insert_dom.
    [Graphical view]
    PANTHERiPTHR11817. PTHR11817. 1 hit.
    PfamiPF00224. PK. 1 hit.
    PF02887. PK_C. 1 hit.
    [Graphical view]
    PRINTSiPR01050. PYRUVTKNASE.
    SUPFAMiSSF50800. SSF50800. 1 hit.
    SSF51621. SSF51621. 2 hits.
    SSF52935. SSF52935. 1 hit.
    TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
    PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiKPYK1_YEAST
    AccessioniPrimary (citable) accession number: P00549
    Secondary accession number(s): D6VPH8, Q2VQG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: September 7, 2016
    This is version 174 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 291000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, 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. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome I
      Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.