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UniProtKB - P16861 (PFKA1_YEAST)

UniProt

P16861 - PFKA1_YEAST

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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

Mg2+UniRule annotationBy similarity

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

    Pathwayi: 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 annotationBy similarity
    Metal bindingi309 – 3091Magnesium; catalyticUniRule annotationBy similarity
    Active sitei356 – 3561Proton acceptorUniRule annotationBy similarity
    Binding sitei391 – 3911Substrate; shared with subunit beta1 Publication
    Binding sitei455 – 4551Substrate1 Publication
    Binding sitei482 – 4821Substrate; shared with subunit beta1 Publication
    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 annotationBy similarity
    Nucleotide bindingi308 – 3114ATPUniRule annotationBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    • 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.
    ReactomeiR-SCE-70171. 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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
    Proteomesi
    • UP000002311 Componenti: Chromosome VII

    Organism-specific databases

    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 – 31PhosphoserineCombined sources
    Cross-linki89 – 89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei166 – 1661PhosphoserineCombined sources
    Modified residuei179 – 1791PhosphoserineCombined sources
    Modified residuei185 – 1851PhosphoserineCombined sources
    Modified residuei189 – 1891PhosphoserineCombined sources
    Modified residuei192 – 1921PhosphoserineCombined sources
    Modified residuei217 – 2171PhosphoserineCombined sources
    Modified residuei450 – 4501PhosphothreonineCombined sources
    Cross-linki625 – 625Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP16861.

    PTM databases

    iPTMnetiP16861.

    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. 226 interactions.
    DIPiDIP-1505N.
    IntActiP16861. 46 interactions.
    MINTiMINT-393741.

    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 1UniRule annotation1 PublicationAdd
    BLAST
    Regioni354 – 3563Substrate bindingUniRule annotation1 Publication
    Regioni398 – 4003Substrate bindingUniRule annotation1 Publication
    Regioni488 – 4914Substrate bindingUniRule annotation1 Publication
    Regioni581 – 59414Interdomain linkerUniRule annotation1 PublicationAdd
    BLAST
    Regioni595 – 987393C-terminal regulatory PFK domain 2UniRule annotation1 PublicationAdd
    BLAST
    Regioni722 – 7265Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation1 Publication
    Regioni767 – 7693Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation1 Publication
    Regioni859 – 8624Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation1 Publication

    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

    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000200154.
    InParanoidiP16861.
    KOiK00850.
    OMAiEVYAIYE.
    OrthoDBiEOG092C0LOE.

    Family and domain databases

    HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
    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. 226 interactions.
    DIPiDIP-1505N.
    IntActiP16861. 46 interactions.
    MINTiMINT-393741.

    PTM databases

    iPTMnetiP16861.

    Proteomic databases

    MaxQBiP16861.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    EuPathDBiFungiDB:YGR240C.
    SGDiS000003472. PFK1.

    Phylogenomic databases

    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000200154.
    InParanoidiP16861.
    KOiK00850.
    OMAiEVYAIYE.
    OrthoDBiEOG092C0LOE.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    BioCyciYEAST:YGR240C-MONOMER.
    ReactomeiR-SCE-70171. Glycolysis.
    SABIO-RKP16861.

    Miscellaneous databases

    PROiP16861.

    Family and domain databases

    HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
    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...

    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: September 7, 2016
    This is version 155 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

    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.