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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfk1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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. May also have a role in cell cycle regulation.UniRule annotation2 Publications

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation1 Publication

Kineticsi

  1. KM=0.025 mM for ATP (without effector)1 Publication
  2. KM=0.027 mM for ATP (with 2.6 µM fructose 2,6-bisphosphate)1 Publication
  3. KM=0.63 mM for fructose 6-phosphate (without effector)1 Publication
  4. KM=0.31 mM for fructose 6-phosphate (with 1 mM AMP)1 Publication
  5. KM=0.17 mM for fructose 6-phosphate (with 2.6 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 (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 sitei204 – 2041ATP; via amide nitrogenUniRule annotation
    Metal bindingi298 – 2981Magnesium; catalyticUniRule annotation
    Active sitei345 – 3451Proton acceptorUniRule annotation
    Binding sitei380 – 3801Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei444 – 4441SubstrateUniRule annotation
    Binding sitei472 – 4721Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei750 – 7501Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei817 – 8171Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei843 – 8431Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei918 – 9181Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi267 – 2682ATPUniRule annotation
    Nucleotide bindingi297 – 3004ATPUniRule annotation

    GO - Molecular functioni

    • 6-phosphofructokinase activity Source: PomBase
    • ATP binding Source: PomBase
    • fructose-6-phosphate binding Source: PomBase
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • canonical glycolysis Source: PomBase
    • carbohydrate phosphorylation Source: GOC
    • fructose 1,6-bisphosphate metabolic process Source: PomBase
    • fructose 6-phosphate metabolic process Source: PomBase
    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

    ReactomeiREACT_304275. Glycolysis.
    SABIO-RKO42938.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PhosphofructokinaseUniRule annotation
    Alternative name(s):
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:pfk1
    ORF Names:SPBC16H5.02
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485 Componenti: Chromosome II

    Organism-specific databases

    EuPathDBiFungiDB:SPBC16H5.02.
    PomBaseiSPBC16H5.02. pfk1.

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    • 6-phosphofructokinase complex Source: PomBase
    • cytoplasm Source: PomBase
    • cytosol Source: PomBase
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 942942ATP-dependent 6-phosphofructokinasePRO_0000112043Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431Phosphoserine1 Publication
    Modified residuei45 – 451Phosphoserine1 Publication
    Modified residuei85 – 851Phosphoserine1 Publication
    Modified residuei160 – 1601Phosphoserine1 Publication
    Modified residuei163 – 1631Phosphoserine1 Publication
    Modified residuei167 – 1671Phosphoserine1 Publication
    Modified residuei171 – 1711Phosphoserine1 Publication
    Modified residuei175 – 1751Phosphothreonine1 Publication
    Modified residuei600 – 6001Phosphoserine1 Publication
    Modified residuei602 – 6021Phosphothreonine1 Publication

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO42938.
    PaxDbiO42938.
    PRIDEiO42938.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Protein-protein interaction databases

    BioGridi276516. 3 interactions.
    MINTiMINT-4674145.
    STRINGi4896.SPBC16H5.02.1.

    Structurei

    3D structure databases

    ProteinModelPortaliO42938.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 570570N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni343 – 3453Substrate bindingUniRule annotation
    Regioni387 – 3893Substrate bindingUniRule annotation
    Regioni478 – 4814Substrate bindingUniRule annotation
    Regioni571 – 58414Interdomain linkerAdd
    BLAST
    Regioni585 – 942358C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni712 – 7165Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni757 – 7593Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni849 – 8524Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

    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.
    HOGENOMiHOG000200154.
    InParanoidiO42938.
    KOiK00850.
    OMAiVYHMASK.
    OrthoDBiEOG7Q5HPV.
    PhylomeDBiO42938.

    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.

    O42938-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSGETVHGIS CYSVVANTED TYNQTLDFYQ KLGFKKVASF GTSDSDNARV
    60 70 80 90 100
    CNESLREDWM HVAGNNSAES VTIKFRLVPG ELSLSPAAED SEWRGQKSSL
    110 120 130 140 150
    VFYYPNLLDL LKQLSADAIK YQAFPNEKKP DEVYVEDPLG NLIGFSDRYN
    160 170 180 190 200
    PFAHANLKKS EESGAASNLE SGLATPVVET LKKATTSDKP AGVKKKIAVM
    210 220 230 240 250
    TSGGDSPGMN AVVRAVARIA IHRGCDAFAI YEGYEGLVQG GDMIKQLQWG
    260 270 280 290 300
    DVRGWLAEGG TLIGTARCMA FRERPGRLRA AKNLISAGID SIIVCGGDGS
    310 320 330 340 350
    LTGADIFRSD WPGLVKELED TKAITPEQAK LYRHLTIVGL VGSIDNDMSS
    360 370 380 390 400
    TDVTIGAFSS LHRICEAVDS ISSTAISHSR AFIVEVMGRH CGWLAVLAAL
    410 420 430 440 450
    ATGADFVFIP ERPAEVGKWQ DELCNSLSSV RKLGKRKSIV IVAEGAIDSE
    460 470 480 490 500
    LNHISPEDIK NLLVERLHLD TRVTTLGHVQ RGGIPCAYDR MLATLQGVDA
    510 520 530 540 550
    VDAVLASTPD TPSPMIAING NKINRKPLME AVKLTHEVAD AIEKKQFAHA
    560 570 580 590 600
    MELRDPEFAD YLHTWEGTTF IEDESHFVPK DERMRVAIIH VGAPAGGMNS
    610 620 630 640 650
    ATRAAVRYCL NRGHTPLAID NGFSGFLRHD SIHELSWIDV DEWCIRGGSE
    660 670 680 690 700
    IGTNRDTPDL DMGFTAFKFQ QHKIDALIII GGFEAFTALS QLESARVNYP
    710 720 730 740 750
    SFRIPMAIIP ATISNNVPGT EFSLGCDTCL NAVMEYCDTI KQSASASRRR
    760 770 780 790 800
    VFVCEVQGGR SGYIATVGGL ITGASAIYTP EDGISLDMLR KDIDHLKATF
    810 820 830 840 850
    ALEAGRNRAG QLILRNECAS KVYTTEVIGN IISEEAHKRF SARTAVPGHV
    860 870 880 890 900
    QQGGNPTPMD RARAARLAMR AIRFFETCRA NDLGNDPSSA VVIGIRGTGV
    910 920 930 940
    SFSSVADVEN NETEIEMRRP KNAWWRDMHN LVNILAGKTF AD
    Length:942
    Mass (Da):102,555
    Last modified:June 1, 1998 - v1
    Checksum:iC6052AF7C1DB75B4
    GO

    Sequence cautioni

    The sequence BAA13773.1 differs from that shown. Reason: Frameshift at position 836. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CU329671 Genomic DNA. Translation: CAA17900.1.
    D89110 mRNA. Translation: BAA13773.1. Frameshift.
    PIRiT39624.
    T42087.
    RefSeqiNP_595946.1. NM_001021854.2.

    Genome annotation databases

    EnsemblFungiiSPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
    GeneIDi2539972.
    KEGGispo:SPBC16H5.02.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CU329671 Genomic DNA. Translation: CAA17900.1.
    D89110 mRNA. Translation: BAA13773.1. Frameshift.
    PIRiT39624.
    T42087.
    RefSeqiNP_595946.1. NM_001021854.2.

    3D structure databases

    ProteinModelPortaliO42938.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi276516. 3 interactions.
    MINTiMINT-4674145.
    STRINGi4896.SPBC16H5.02.1.

    Proteomic databases

    MaxQBiO42938.
    PaxDbiO42938.
    PRIDEiO42938.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiSPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
    GeneIDi2539972.
    KEGGispo:SPBC16H5.02.

    Organism-specific databases

    EuPathDBiFungiDB:SPBC16H5.02.
    PomBaseiSPBC16H5.02. pfk1.

    Phylogenomic databases

    eggNOGiCOG0205.
    HOGENOMiHOG000200154.
    InParanoidiO42938.
    KOiK00850.
    OMAiVYHMASK.
    OrthoDBiEOG7Q5HPV.
    PhylomeDBiO42938.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    ReactomeiREACT_304275. Glycolysis.
    SABIO-RKO42938.

    Miscellaneous databases

    NextBioi20801115.
    PROiO42938.

    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. "Analysis of 114 kb of DNA sequence from fission yeast chromosome 2 immediately centromere-distal to his5."
      Xiang Z., Moore K., Wood V., Rajandream M.A., Barrell B.G., Skelton J., Churcher C.M., Lyne M.H., Devlin K., Gwilliam R., Rutherford K.M., Aves S.J.
      Yeast 16:1405-1411(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
      Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
      DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-942.
      Strain: PR745.
    4. "Purification, molecular and kinetic characterization of phosphofructokinase-1 from the yeast Schizosaccharomyces pombe: evidence for an unusual subunit composition."
      Reuter R., Naumann M., Baer J., Haferburg D., Kopperschlaeger G.
      Yeast 16:1273-1285(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 182-190 AND 552-558, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: CBS 1057.
    5. "Genome-wide search of Schizosaccharomyces pombe genes causing overexpression-mediated cell cycle defects."
      Tallada V.A., Daga R.R., Palomeque C., Garzon A., Jimenez J.
      Yeast 19:1139-1151(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL CYCLE REGULATION.
    6. "Structures of S. pombe phosphofructokinase in the F6P-bound and ATP-bound states."
      Benjamin S., Radermacher M., Baer J., Edelmann A., Ruiz T.
      J. Struct. Biol. 159:498-506(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45; SER-85; SER-160; SER-163; SER-167; SER-171; THR-175; SER-600 AND THR-602, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiPFKA_SCHPO
    AccessioniPrimary (citable) accession number: O42938
    Secondary accession number(s): P78762
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: June 1, 1998
    Last modified: June 24, 2015
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    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.