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Protein

ATP-dependent 6-phosphofructokinase subunit beta

Gene

PFK2

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

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation8 Publications

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation1 Publication

Cofactori

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation3 Publications

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

    Pathway:iglycolysis

    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. no protein annotated in this organism
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei206 – 2061ATP; via amide nitrogenUniRule annotation
    Metal bindingi301 – 3011Magnesium; catalytic
    Active sitei348 – 3481Proton acceptor
    Binding sitei383 – 3831Substrate; shared with subunit alpha
    Binding sitei447 – 4471Substrate
    Binding sitei475 – 4751Substrate; shared with subunit alpha
    Binding sitei658 – 6581Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 Publication
    Binding sitei754 – 7541Allosteric activator fructose 2,6-bisphosphate; shared with subunit alphaUniRule annotation
    Binding sitei847 – 8471Allosteric activator fructose 2,6-bisphosphate; shared with subunit alphaUniRule annotation
    Binding sitei935 – 9351Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi270 – 2712ATPUniRule annotation
    Nucleotide bindingi300 – 3034ATPUniRule annotation

    GO - Molecular functioni

    • 6-phosphofructokinase activity Source: SGD
    • ATP binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • mRNA binding Source: SGD

    GO - Biological processi

    • carbohydrate phosphorylation Source: GOC
    • fructose 6-phosphate metabolic process Source: InterPro
    • glycolytic process Source: SGD
    • hydrogen ion transmembrane transport Source: GOC
    • proton transport Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YMR205C-MONOMER.
    BRENDAi2.7.1.11. 984.
    ReactomeiREACT_275254. Glycolysis.
    SABIO-RKP16862.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase subunit betaUniRule annotation (EC:2.7.1.11UniRule annotation)
    Alternative name(s):
    ATP-dependent 6-phosphofructokinaseUniRule annotation
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    Phosphofructokinase 2UniRule annotation
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:PFK2
    Ordered Locus Names:YMR205C
    ORF Names:YM8325.06C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XIII

    Organism-specific databases

    EuPathDBiFungiDB:YMR205C.
    SGDiS000004818. PFK2.

    Subcellular locationi

    GO - Cellular componenti

    • 6-phosphofructokinase complex Source: SGD
    • mitochondrial outer membrane Source: UniProtKB-SubCell
    • mitochondrion Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi301 – 3011D → T: Reduces maximal activity of the holoenzyme by 30%. 1 Publication
    Mutagenesisi348 – 3481D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'T-309' or 'S-356' in subunit alpha. 1 Publication
    Mutagenesisi439 – 4391R → V: Reduces maximal activity of the holoenzyme by less than 25%. 1 Publication
    Mutagenesisi481 – 4811H → S: Increases the KM for fructose 6-phosphate 50 fold. 1 Publication
    Mutagenesisi718 – 7181S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-724' in subunit alpha. 1 Publication
    Mutagenesisi722 – 7221P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. 1 Publication
    Mutagenesisi853 – 8531H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-859' in subunit alpha. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 959958ATP-dependent 6-phosphofructokinase subunit betaPRO_0000112046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521Phosphothreonine1 Publication
    Modified residuei163 – 1631Phosphoserine2 Publications
    Modified residuei171 – 1711Phosphoserine2 Publications
    Modified residuei803 – 8031Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16862.
    PaxDbiP16862.
    PeptideAtlasiP16862.

    Interactioni

    Subunit structurei

    Heterooctamer of 4 alpha and 4 beta chains.UniRule annotation3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PFK1P168614EBI-9435,EBI-9428
    RSP5P399403EBI-9435,EBI-16219

    Protein-protein interaction databases

    BioGridi35383. 172 interactions.
    DIPiDIP-2619N.
    IntActiP16862. 44 interactions.
    MINTiMINT-424355.

    Structurei

    Secondary structure

    1
    959
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi198 – 2069Combined sources
    Helixi211 – 22515Combined sources
    Beta strandi228 – 2325Combined sources
    Helixi235 – 2406Combined sources
    Turni244 – 2463Combined sources
    Beta strandi247 – 2504Combined sources
    Helixi252 – 2554Combined sources
    Helixi258 – 2603Combined sources
    Helixi273 – 2753Combined sources
    Helixi277 – 28913Combined sources
    Beta strandi294 – 2996Combined sources
    Helixi301 – 32222Combined sources
    Beta strandi325 – 3273Combined sources
    Helixi329 – 3346Combined sources
    Beta strandi339 – 3457Combined sources
    Helixi360 – 38021Combined sources
    Beta strandi384 – 3896Combined sources
    Helixi396 – 40510Combined sources
    Beta strandi408 – 4114Combined sources
    Helixi421 – 43515Combined sources
    Beta strandi441 – 4466Combined sources
    Helixi459 – 46810Combined sources
    Beta strandi474 – 4785Combined sources
    Helixi480 – 4834Combined sources
    Helixi490 – 50920Combined sources
    Beta strandi517 – 5248Combined sources
    Beta strandi526 – 5305Combined sources
    Helixi531 – 54616Combined sources
    Helixi550 – 5567Combined sources
    Helixi561 – 57313Combined sources
    Beta strandi581 – 5844Combined sources
    Beta strandi588 – 5969Combined sources
    Helixi601 – 61515Combined sources
    Beta strandi618 – 6225Combined sources
    Helixi625 – 6328Combined sources
    Beta strandi635 – 6373Combined sources
    Helixi640 – 6434Combined sources
    Helixi646 – 6483Combined sources
    Helixi661 – 6644Combined sources
    Helixi666 – 67611Combined sources
    Beta strandi679 – 6868Combined sources
    Helixi687 – 69711Combined sources
    Turni698 – 7025Combined sources
    Helixi704 – 7063Combined sources
    Beta strandi712 – 7154Combined sources
    Helixi730 – 75122Combined sources
    Beta strandi752 – 7609Combined sources
    Helixi767 – 77610Combined sources
    Beta strandi779 – 7824Combined sources
    Turni784 – 7863Combined sources
    Helixi790 – 80718Combined sources
    Beta strandi815 – 8206Combined sources
    Helixi821 – 8233Combined sources
    Helixi829 – 84012Combined sources
    Beta strandi845 – 8506Combined sources
    Helixi852 – 8565Combined sources
    Helixi862 – 88120Combined sources
    Helixi884 – 8896Combined sources
    Beta strandi890 – 8945Combined sources
    Helixi901 – 9044Combined sources
    Beta strandi907 – 9115Combined sources
    Beta strandi913 – 9153Combined sources
    Beta strandi918 – 9214Combined sources
    Helixi922 – 9287Combined sources
    Helixi932 – 9343Combined sources
    Beta strandi935 – 9395Combined sources
    Helixi943 – 95210Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O8OX-ray2.90B/D/F/H194-959[»]
    ProteinModelPortaliP16862.
    SMRiP16862. Positions 9-957.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 573572N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni346 – 3483Substrate binding
    Regioni390 – 3923Substrate binding
    Regioni481 – 4844Substrate binding
    Regioni574 – 58714Interdomain linkerAdd
    BLAST
    Regioni588 – 959372C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni716 – 7205Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni716 – 7183Allosteric activator fructose 2,6-bisphosphate binding
    Regioni761 – 7633Allosteric activator fructose 2,6-bisphosphate binding
    Regioni853 – 8564Allosteric activator fructose 2,6-bisphosphate binding

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0205.
    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000200154.
    InParanoidiP16862.
    KOiK00850.
    OMAiIRQLYDY.
    OrthoDBiEOG7Q5HPV.

    Family and domain databases

    Gene3Di3.10.180.10. 1 hit.
    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-Pfructokinase_euk.
    IPR022953. ATP_PFK.
    IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 2 hits.
    SSF54593. SSF54593. 1 hit.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16862-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVTTPFVNG TSYCTVTAYS VQSYKAAIDF YTKFLSLENR SSPDENSTLL
    60 70 80 90 100
    SNDSISLKIL LRPDEKINKN VEAHLKELNS ITKTQDWRSH ATQSLVFNTS
    110 120 130 140 150
    DILAVKDTLN AMNAPLQGYP TELFPMQLYT LDPLGNVVGV TSTKNAVSTK
    160 170 180 190 200
    PTPPPAPEAS AESGLSSKVH SYTDLAYRMK TTDTYPSLPK PLNRPQKAIA
    210 220 230 240 250
    VMTSGGDAPG MNSNVRAIVR SAIFKGCRAF VVMEGYEGLV RGGPEYIKEF
    260 270 280 290 300
    HWEDVRGWSA EGGTNIGTAR CMEFKKREGR LLGAQHLIEA GVDALIVCGG
    310 320 330 340 350
    DGSLTGADLF RSEWPSLIEE LLKTNRISNE QYERMKHLNI CGTVGSIDND
    360 370 380 390 400
    MSTTDATIGA YSALDRICKA IDYVEATANS HSRAFVVEVM GRNCGWLALL
    410 420 430 440 450
    AGIATSADYI FIPEKPATSS EWQDQMCDIV SKHRSRGKRT TIVVVAEGAI
    460 470 480 490 500
    AADLTPISPS DVHKVLVDRL GLDTRITTLG HVQRGGTAVA YDRILATLQG
    510 520 530 540 550
    LEAVNAVLES TPDTPSPLIA VNENKIVRKP LMESVKLTKA VAEAIQAKDF
    560 570 580 590 600
    KRAMSLRDTE FIEHLNNFMA INSADHNEPK LPKDKRLKIA IVNVGAPAGG
    610 620 630 640 650
    INSAVYSMAT YCMSQGHRPY AIYNGWSGLA RHESVRSLNW KDMLGWQSRG
    660 670 680 690 700
    GSEIGTNRVT PEEADLGMIA YYFQKYEFDG LIIVGGFEAF ESLHQLERAR
    710 720 730 740 750
    ESYPAFRIPM VLIPATLSNN VPGTEYSLGS DTALNALMEY CDVVKQSASS
    760 770 780 790 800
    TRGRAFVVDC QGGNSGYLAT YASLAVGAQV SYVPEEGISL EQLSEDIEYL
    810 820 830 840 850
    AQSFEKAEGR GRFGKLILKS TNASKALSAT KLAEVITAEA DGRFDAKPAY
    860 870 880 890 900
    PGHVQQGGLP SPIDRTRATR MAIKAVGFIK DNQAAIAEAR AAEENFNADD
    910 920 930 940 950
    KTISDTAAVV GVKGSHVVYN SIRQLYDYET EVSMRMPKVI HWQATRLIAD

    HLVGRKRVD
    Length:959
    Mass (Da):104,618
    Last modified:January 23, 2007 - v4
    Checksum:i82CE6402CEDBBCB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371V → G in AAA34860 (PubMed:2528496).Curated
    Sequence conflicti880 – 8801K → E in AAA34860 (PubMed:2528496).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M26944 Genomic DNA. Translation: AAA34860.1.
    Z48755 Genomic DNA. Translation: CAA88646.1.
    BK006946 Genomic DNA. Translation: DAA10104.1.
    PIRiS59446. JQ0017.
    RefSeqiNP_013932.1. NM_001182712.1.

    Genome annotation databases

    EnsemblFungiiYMR205C; YMR205C; YMR205C.
    GeneIDi855245.
    KEGGisce:YMR205C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M26944 Genomic DNA. Translation: AAA34860.1.
    Z48755 Genomic DNA. Translation: CAA88646.1.
    BK006946 Genomic DNA. Translation: DAA10104.1.
    PIRiS59446. JQ0017.
    RefSeqiNP_013932.1. NM_001182712.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O8OX-ray2.90B/D/F/H194-959[»]
    ProteinModelPortaliP16862.
    SMRiP16862. Positions 9-957.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35383. 172 interactions.
    DIPiDIP-2619N.
    IntActiP16862. 44 interactions.
    MINTiMINT-424355.

    Proteomic databases

    MaxQBiP16862.
    PaxDbiP16862.
    PeptideAtlasiP16862.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYMR205C; YMR205C; YMR205C.
    GeneIDi855245.
    KEGGisce:YMR205C.

    Organism-specific databases

    EuPathDBiFungiDB:YMR205C.
    SGDiS000004818. PFK2.

    Phylogenomic databases

    eggNOGiCOG0205.
    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000200154.
    InParanoidiP16862.
    KOiK00850.
    OMAiIRQLYDY.
    OrthoDBiEOG7Q5HPV.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    BioCyciYEAST:YMR205C-MONOMER.
    BRENDAi2.7.1.11. 984.
    ReactomeiREACT_275254. Glycolysis.
    SABIO-RKP16862.

    Miscellaneous databases

    NextBioi978807.
    PROiP16862.

    Family and domain databases

    Gene3Di3.10.180.10. 1 hit.
    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-Pfructokinase_euk.
    IPR022953. ATP_PFK.
    IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 2 hits.
    SSF54593. SSF54593. 1 hit.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The phosphofructokinase genes of yeast evolved from two duplication events."
      Heinisch J.J., Ritzel R.G., von Borstel R.C., Aguilera A., Rodicio R., Zimmermann F.K.
      Gene 78:309-321(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases."
      Kopperschlaeger G., Baer J., Stellwagen E.
      Eur. J. Biochem. 217:527-533(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12; 181-185 AND 193-197.
    5. "Physicochemical parameters and subunit composition of yeast phosphofructokinase."
      Kopperschlaeger G., Baer J., Nissler K., Hofmann E.
      Eur. J. Biochem. 81:317-325(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    6. "Activation by phosphate of yeast phosphofructokinase."
      Banuelos M., Gancedo C., Gancedo J.M.
      J. Biol. Chem. 252:6394-6398(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "Phosphorus-31 nuclear magnetic resonance studies of wild-type and glycolytic pathway mutants of Saccharomyces cerevisiae."
      Navon G., Shulman R.G., Yamane T., Eccleshall T.R., Lam K.B., Baronofsky J.J., Marmur J.
      Biochemistry 18:4487-4499(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Stimulation of yeast phosphofructokinase activity by fructose 2,6-bisphosphate."
      Avigad G.
      Biochem. Biophys. Res. Commun. 102:985-991(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "Mutant studies of yeast phosphofructokinase."
      Clifton D., Fraenkel D.G.
      Biochemistry 21:1935-1942(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Similarity of activation of yeast phosphofructokinase by AMP and fructose-2,6-bisphosphate."
      Nissler K., Otto A., Schellenberger W., Hofmann E.
      Biochem. Biophys. Res. Commun. 111:294-300(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    11. "Temporal organization of the phosphofructokinase/fructose-1,6-biphosphatase cycle."
      Hofmann E., Eschrich K., Schellenberger W.
      Adv. Enzyme Regul. 23:331-362(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "An electron microscopy study of the quarternary structure of yeast phosphofructokinase."
      Nissler K., Hofmann E., Stel'maschchuk V., Orlova E., Kiselev N.
      Biomed. Biochim. Acta 44:251-259(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    13. "Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast."
      Heinisch J.
      Mol. Gen. Genet. 202:75-82(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis."
      Arvanitidis A., Heinisch J.J.
      J. Biol. Chem. 269:8911-8918(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-301; ASP-348; ARG-439 AND HIS-481.
    15. "A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control."
      Heinisch J.J., Boles E., Timpel C.
      J. Biol. Chem. 271:15928-15933(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-718 AND HIS-853.
    16. "Single point mutations in either gene encoding the subunits of the heterooctameric yeast phosphofructokinase abolish allosteric inhibition by ATP."
      Rodicio R., Strauss A., Heinisch J.J.
      J. Biol. Chem. 275:40952-40960(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PRO-722.
    17. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    19. Cited for: SUBCELLULAR LOCATION.
    20. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    21. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Detection and localisation of protein-protein interactions in Saccharomyces cerevisiae using a split-GFP method."
      Barnard E., McFerran N.V., Trudgett A., Nelson J., Timson D.J.
      Fungal Genet. Biol. 45:597-604(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    23. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152; SER-163 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle."
      Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T., Radermacher M., Kopperschlager G., Rypniewski W.
      J. Mol. Biol. 407:284-297(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959 IN COMPLEX WITH SUBSTRATE FRUCTOSE 6-PHOSPHATE AND ALLOSTERIC ACTIVATOR FRUCTOSE 2,6-BISPHOSPHATE.

    Entry informationi

    Entry nameiPFKA2_YEAST
    AccessioniPrimary (citable) accession number: P16862
    Secondary accession number(s): D6W030
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: July 22, 2015
    This is version 158 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 90200 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3

    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 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.