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Protein

Pyruvate kinase 1

Gene

CDC19

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

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

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 1 (ERR1), Enolase-related protein 3 (ERR3), 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)DescriptionActionsGraphical viewLength
    Binding sitei49SubstrateCombined sources1 Publication1
    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
    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

    GO - Molecular functioni

    GO - Biological processi

    • glycolytic process Source: SGD
    • pyruvate metabolic process Source: SGD

    Keywordsi

    Molecular functionAllosteric enzyme, Kinase, Transferase
    Biological processGlycolysis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

    Enzyme and pathway databases

    BioCyciYEAST:YAL038W-MONOMER
    ReactomeiR-SCE-6798695 Neutrophil degranulation
    R-SCE-70171 Glycolysis
    SABIO-RKiP00549
    UniPathwayiUPA00109; UER00188

    Protein family/group databases

    MoonProtiP00549

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi240K → M: Reduces activity 1000-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00001121212 – 500Pyruvate kinase 1Add BLAST499

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineCombined sources1
    Modified residuei9PhosphoserineCombined sources1
    Modified residuei16PhosphoserineCombined sources1
    Modified residuei31PhosphothreonineCombined sources1
    Modified residuei70PhosphoserineCombined sources1
    Modified residuei184PhosphothreonineCombined sources1
    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

    MaxQBiP00549
    PaxDbiP00549
    PRIDEiP00549
    TopDownProteomicsiP00549

    2D gel databases

    COMPLUYEAST-2DPAGEiP00549

    PTM databases

    CarbonylDBiP00549
    iPTMnetiP00549

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi31727, 262 interactors
    DIPiDIP-4124N
    ELMiP00549
    IntActiP00549, 200 interactors
    MINTiP00549
    STRINGi4932.YAL038W

    Structurei

    Secondary structure

    1500
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 8Combined sources6
    Beta strandi21 – 26Combined sources6
    Helixi29 – 31Combined sources3
    Helixi34 – 43Combined sources10
    Beta strandi47 – 49Combined sources3
    Helixi57 – 73Combined sources17
    Beta strandi82 – 84Combined sources3
    Beta strandi96 – 99Combined sources4
    Beta strandi108 – 112Combined sources5
    Turni116 – 120Combined sources5
    Beta strandi126 – 129Combined sources4
    Helixi133 – 136Combined sources4
    Beta strandi142 – 145Combined sources4
    Turni146 – 149Combined sources4
    Beta strandi150 – 153Combined sources4
    Turni159 – 161Combined sources3
    Beta strandi163 – 167Combined sources5
    Beta strandi178 – 180Combined sources3
    Helixi193 – 205Combined sources13
    Beta strandi208 – 212Combined sources5
    Helixi218 – 232Combined sources15
    Beta strandi235 – 241Combined sources7
    Helixi245 – 248Combined sources4
    Helixi250 – 256Combined sources7
    Beta strandi260 – 262Combined sources3
    Helixi264 – 270Combined sources7
    Helixi273 – 275Combined sources3
    Helixi276 – 290Combined sources15
    Beta strandi294 – 296Combined sources3
    Helixi302 – 305Combined sources4
    Helixi312 – 324Combined sources13
    Beta strandi327 – 329Combined sources3
    Turni333 – 337Combined sources5
    Helixi341 – 355Combined sources15
    Beta strandi357 – 359Combined sources3
    Helixi361 – 368Combined sources8
    Helixi378 – 393Combined sources16
    Beta strandi398 – 401Combined sources4
    Beta strandi403 – 405Combined sources3
    Helixi406 – 413Combined sources8
    Beta strandi420 – 425Combined sources6
    Helixi429 – 432Combined sources4
    Helixi433 – 435Combined sources3
    Beta strandi439 – 443Combined sources5
    Turni452 – 454Combined sources3
    Helixi455 – 469Combined sources15
    Beta strandi478 – 483Combined sources6
    Turni487 – 489Combined sources3
    Beta strandi494 – 499Combined sources6

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP00549

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni402 – 407Allosteric activator bindingCombined sources1 Publication6

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000008859
    HOGENOMiHOG000021559
    InParanoidiP00549
    KOiK00873
    OMAiKHEAIEQ
    OrthoDBiEOG092C1RXZ

    Family and domain databases

    CDDicd00288 Pyruvate_Kinase, 1 hit
    Gene3Di2.40.33.10, 1 hit
    3.40.1380.20, 2 hits
    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, 2 hits
    SSF52935 SSF52935, 1 hit
    TIGRFAMsiTIGR01064 pyruv_kin, 1 hit
    PROSITEiView protein in PROSITE
    PS00110 PYRUVATE_KINASE, 1 hit

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti382 – 386VAASA → SLPR in CAA24631 (PubMed:2653861).Curated5

    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

    Similar proteinsi

    Entry informationi

    Entry nameiKPYK1_YEAST
    AccessioniPrimary (citable) accession number: P00549
    Secondary accession number(s): D6VPH8, Q2VQG5
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: April 25, 2018
    This is version 192 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health