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Protein

ATP-dependent 6-phosphofructokinase subunit alpha

Gene

PFK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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: glycolysis

    This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. 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 sitei215 – 2151ATP; via amide nitrogenUniRule annotation
    Metal bindingi309 – 3091Magnesium; catalytic
    Active sitei356 – 3561Proton acceptor
    Binding sitei391 – 3911Substrate; shared with subunit beta
    Binding sitei455 – 4551Substrate
    Binding sitei482 – 4821Substrate; shared with subunit beta
    Binding sitei665 – 6651Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 Publication
    Binding sitei760 – 7601Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation1 Publication
    Binding sitei827 – 8271Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 Publication
    Binding sitei853 – 8531Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation1 Publication
    Binding sitei952 – 9521Allosteric activator fructose 2,6-bisphosphateUniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi278 – 2792ATPUniRule annotation
    Nucleotide bindingi308 – 3114ATPUniRule annotation

    GO - Molecular functioni

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

    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:YGR240C-MONOMER.
    ReactomeiREACT_275254. Glycolysis.
    SABIO-RKP16861.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase subunit alphaUniRule annotation (EC:2.7.1.11UniRule annotation)
    Alternative name(s):
    ATP-dependent 6-phosphofructokinaseUniRule annotation
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    Phosphofructokinase 1UniRule annotation
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:PFK1
    Ordered Locus Names:YGR240C
    ORF Names:G8599
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome VII

    Organism-specific databases

    CYGDiYGR240c.
    EuPathDBiFungiDB:YGR240C.
    SGDiS000003472. PFK1.

    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
    Mutagenesisi309 – 3091D → T: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. 1 Publication
    Mutagenesisi356 – 3561D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. 1 Publication
    Mutagenesisi447 – 4471R → S: Reduces maximal activity of the holoenzyme by less than 25%. 1 Publication
    Mutagenesisi488 – 4881H → S: Increases the KM for fructose 6-phosphate 20 fold. 1 Publication
    Mutagenesisi724 – 7241S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-718' in subunit beta. 1 Publication
    Mutagenesisi728 – 7281P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. 1 Publication
    Mutagenesisi859 – 8591H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-853' in subunit beta. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 987987ATP-dependent 6-phosphofructokinase subunit alphaPRO_0000112045Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Phosphoserine1 Publication
    Modified residuei166 – 1661Phosphoserine1 Publication
    Modified residuei179 – 1791Phosphoserine2 Publications
    Modified residuei185 – 1851Phosphoserine3 Publications
    Modified residuei189 – 1891Phosphoserine1 Publication
    Modified residuei192 – 1921Phosphoserine3 Publications
    Modified residuei217 – 2171Phosphoserine1 Publication
    Modified residuei450 – 4501Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16861.
    PaxDbiP16861.
    PeptideAtlasiP16861.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PFK2P168624EBI-9428,EBI-9435

    Protein-protein interaction databases

    BioGridi33492. 225 interactions.
    DIPiDIP-1505N.
    IntActiP16861. 46 interactions.
    MINTiMINT-393741.
    STRINGi4932.YGR240C.

    Structurei

    Secondary structure

    1
    987
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi207 – 2159Combined sources
    Helixi220 – 23314Combined sources
    Beta strandi237 – 2415Combined sources
    Helixi244 – 2507Combined sources
    Beta strandi254 – 2574Combined sources
    Helixi260 – 2634Combined sources
    Helixi266 – 2683Combined sources
    Helixi281 – 2833Combined sources
    Helixi285 – 29713Combined sources
    Beta strandi300 – 3078Combined sources
    Helixi309 – 31911Combined sources
    Helixi322 – 3309Combined sources
    Beta strandi331 – 3344Combined sources
    Turni337 – 3437Combined sources
    Beta strandi347 – 35610Combined sources
    Helixi368 – 38821Combined sources
    Beta strandi392 – 3976Combined sources
    Helixi404 – 4129Combined sources
    Beta strandi416 – 4194Combined sources
    Helixi421 – 4233Combined sources
    Turni427 – 4293Combined sources
    Helixi430 – 44314Combined sources
    Beta strandi449 – 4546Combined sources
    Helixi467 – 47711Combined sources
    Beta strandi481 – 4855Combined sources
    Helixi487 – 4904Combined sources
    Helixi497 – 51519Combined sources
    Beta strandi524 – 53714Combined sources
    Helixi538 – 55316Combined sources
    Helixi557 – 5626Combined sources
    Helixi568 – 57912Combined sources
    Beta strandi595 – 6039Combined sources
    Helixi608 – 62215Combined sources
    Beta strandi625 – 6295Combined sources
    Helixi632 – 6398Combined sources
    Beta strandi642 – 6443Combined sources
    Turni647 – 6526Combined sources
    Helixi653 – 6553Combined sources
    Helixi668 – 6703Combined sources
    Helixi672 – 68110Combined sources
    Beta strandi685 – 6928Combined sources
    Helixi693 – 70513Combined sources
    Turni706 – 7083Combined sources
    Helixi710 – 7134Combined sources
    Beta strandi716 – 7216Combined sources
    Helixi736 – 75722Combined sources
    Beta strandi758 – 7669Combined sources
    Helixi773 – 7808Combined sources
    Turni781 – 7833Combined sources
    Beta strandi785 – 7884Combined sources
    Beta strandi790 – 7923Combined sources
    Helixi796 – 81217Combined sources
    Beta strandi821 – 8266Combined sources
    Beta strandi831 – 8333Combined sources
    Helixi835 – 84612Combined sources
    Beta strandi849 – 8568Combined sources
    Helixi858 – 8625Combined sources
    Helixi868 – 89023Combined sources
    Helixi921 – 9233Combined sources
    Beta strandi924 – 9307Combined sources
    Beta strandi933 – 9386Combined sources
    Helixi939 – 9424Combined sources
    Turni948 – 9514Combined sources
    Beta strandi953 – 9553Combined sources
    Helixi960 – 96910Combined sources
    Helixi972 – 9787Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O8OX-ray2.90A/C/E/G201-987[»]
    ProteinModelPortaliP16861.
    SMRiP16861. Positions 10-980.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 580580N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni354 – 3563Substrate binding
    Regioni398 – 4003Substrate binding
    Regioni488 – 4914Substrate binding
    Regioni581 – 59414Interdomain linkerAdd
    BLAST
    Regioni595 – 987393C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni722 – 7265Allosteric activator fructose 2,6-bisphosphate binding
    Regioni767 – 7693Allosteric activator fructose 2,6-bisphosphate binding
    Regioni859 – 8624Allosteric 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.
    InParanoidiP16861.
    KOiK00850.
    OMAiKMCQKLS.
    OrthoDBiEOG7Q5HPV.

    Family and domain databases

    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-Pfructokinase_euk.
    IPR022953. ATP_PFK.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 3 hits.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16861-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQSQDSCYGV AFRSIITNDE ALFKKTIHFY HTLGFATVKD FNKFKHGENS
    60 70 80 90 100
    LLSSGTSQDS LREVWLESFK LSEVDASGFR IPQQEATNKA QSQGALLKIR
    110 120 130 140 150
    LVMSAPIDET FDTNETATIT YFSTDLNKIV EKFPKQAEKL SDTLVFLKDP
    160 170 180 190 200
    MGNNITFSGL ANATDSAPTS KDAFLEATSE DEIISRASSD ASDLLRQTLG
    210 220 230 240 250
    SSQKKKKIAV MTSGGDSPGM NAAVRAVVRT GIHFGCDVFA VYEGYEGLLR
    260 270 280 290 300
    GGKYLKKMAW EDVRGWLSEG GTLIGTARSM EFRKREGRRQ AAGNLISQGI
    310 320 330 340 350
    DALVVCGGDG SLTGADLFRH EWPSLVDELV AEGRFTKEEV APYKNLSIVG
    360 370 380 390 400
    LVGSIDNDMS GTDSTIGAYS ALERICEMVD YIDATAKSHS RAFVVEVMGR
    410 420 430 440 450
    HCGWLALMAG IATGADYIFI PERAVPHGKW QDELKEVCQR HRSKGRRNNT
    460 470 480 490 500
    IIVAEGALDD QLNPVTANDV KDALIELGLD TKVTILGHVQ RGGTAVAHDR
    510 520 530 540 550
    WLATLQGVDA VKAVLEFTPE TPSPLIGILE NKIIRMPLVE SVKLTKSVAT
    560 570 580 590 600
    AIENKDFDKA ISLRDTEFIE LYENFLSTTV KDDGSELLPV SDRLNIGIVH
    610 620 630 640 650
    VGAPSAALNA ATRAATLYCL SHGHKPYAIM NGFSGLIQTG EVKELSWIDV
    660 670 680 690 700
    ENWHNLGGSE IGTNRSVASE DLGTIAYYFQ KNKLDGLIIL GGFEGFRSLK
    710 720 730 740 750
    QLRDGRTQHP IFNIPMCLIP ATVSNNVPGT EYSLGVDTCL NALVNYTDDI
    760 770 780 790 800
    KQSASATRRR VFVCEVQGGH SGYIASFTGL ITGAVSVYTP EKKIDLASIR
    810 820 830 840 850
    EDITLLKENF RHDKGENRNG KLLVRNEQAS SVYSTQLLAD IISEASKGKF
    860 870 880 890 900
    GVRTAIPGHV QQGGVPSSKD RVTASRFAVK CIKFIEQWNK KNEASPNTDA
    910 920 930 940 950
    KVLRFKFDTH GEKVPTVEHE DDSAAVICVN GSHVSFKPIA NLWENETNVE
    960 970 980
    LRKGFEVHWA EYNKIGDILS GRLKLRAEVA ALAAENK
    Length:987
    Mass (Da):107,970
    Last modified:August 1, 1990 - v1
    Checksum:i995B3DF7C7781B29
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M26943 Genomic DNA. Translation: AAA34859.1.
    Z73025 Genomic DNA. Translation: CAA97268.1.
    X87941 Genomic DNA. Translation: CAA61193.1.
    BK006941 Genomic DNA. Translation: DAA08331.1.
    PIRiJQ0016.
    RefSeqiNP_011756.1. NM_001181369.1.

    Genome annotation databases

    EnsemblFungiiYGR240C; YGR240C; YGR240C.
    GeneIDi853155.
    KEGGisce:YGR240C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M26943 Genomic DNA. Translation: AAA34859.1.
    Z73025 Genomic DNA. Translation: CAA97268.1.
    X87941 Genomic DNA. Translation: CAA61193.1.
    BK006941 Genomic DNA. Translation: DAA08331.1.
    PIRiJQ0016.
    RefSeqiNP_011756.1. NM_001181369.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O8OX-ray2.90A/C/E/G201-987[»]
    ProteinModelPortaliP16861.
    SMRiP16861. Positions 10-980.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33492. 225 interactions.
    DIPiDIP-1505N.
    IntActiP16861. 46 interactions.
    MINTiMINT-393741.
    STRINGi4932.YGR240C.

    Proteomic databases

    MaxQBiP16861.
    PaxDbiP16861.
    PeptideAtlasiP16861.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR240C; YGR240C; YGR240C.
    GeneIDi853155.
    KEGGisce:YGR240C.

    Organism-specific databases

    CYGDiYGR240c.
    EuPathDBiFungiDB:YGR240C.
    SGDiS000003472. PFK1.

    Phylogenomic databases

    eggNOGiCOG0205.
    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000200154.
    InParanoidiP16861.
    KOiK00850.
    OMAiKMCQKLS.
    OrthoDBiEOG7Q5HPV.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    BioCyciYEAST:YGR240C-MONOMER.
    ReactomeiREACT_275254. Glycolysis.
    SABIO-RKP16861.

    Miscellaneous databases

    NextBioi973249.
    PROiP16861.

    Family and domain databases

    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-Pfructokinase_euk.
    IPR022953. ATP_PFK.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 3 hits.
    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. "Sequencing of a 9.9 kb segment on the right arm of yeast chromosome VII reveals four open reading frames, including PFK1, the gene coding for succinyl-CoA synthetase (beta-chain) and two ORFs sharing homology with ORFs of the yeast chromosome VIII."
      Guerreiro P., Azevedo D., Barreiros T., Rodrigues-Pousada C.
      Yeast 13:275-280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII."
      van der Aart Q.J.M., Kleine K., Steensma H.Y.
      Yeast 12:385-390(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 794-987.
      Strain: ATCC 204508 / S288c.
    6. "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 1-6; 90-97; 197-205 AND 914-921.
    7. "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.
    8. "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.
    9. "Glycolysis mutants in Saccharomyces cerevisiae."
      Clifton D., Weinstock S.B., Fraenkel D.G.
      Genetics 88:1-11(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "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.
    11. "Mutant studies of yeast phosphofructokinase."
      Clifton D., Fraenkel D.G.
      Biochemistry 21:1935-1942(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "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.
    13. "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.
    14. "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.
    15. "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.
    16. "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-309; ASP-356; ARG-447 AND HIS-488.
    17. "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-724 AND HIS-859.
    18. "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-728.
    19. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    20. "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.
    21. Cited for: SUBCELLULAR LOCATION.
    22. "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-179; SER-185 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    23. "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.
    24. "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-3; SER-185 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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 SER-166; SER-179; SER-185; SER-189; SER-192; SER-217 AND THR-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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 201-987 IN COMPLEX WITH SUBSTRATE FRUCTOSE 6-PHOSPHATE AND ALLOSTERIC ACTIVATOR FRUCTOSE 2,6-BISPHOSPHATE.

    Entry informationi

    Entry nameiPFKA1_YEAST
    AccessioniPrimary (citable) accession number: P16861
    Secondary accession number(s): D6VV20
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: June 24, 2015
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 89800 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: 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.