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Protein

ATP-dependent 6-phosphofructokinase

Gene

PFK

Organism
Schistosoma mansoni (Blood fluke)
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 annotation1 Publication

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation2 Publications

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=3.5 mM for ATP1 Publication
  2. KM=0.8 mM for fructose 6-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.5-9.0.1 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 (Smp_022400)
    3. ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (Smp_043670.1), ATP-dependent 6-phosphofructokinase (Smp_043670.2)
    4. Fructose-bisphosphate aldolase (Smp_042160.1), Fructose-bisphosphate aldolase (Smp_042160.1), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (Smp_042160.2), Fructose-bisphosphate aldolase (Smp_042160.2)
    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 sitei27 – 271ATP; via amide nitrogenUniRule annotation
    Metal bindingi121 – 1211Magnesium; catalyticUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei203 – 2031Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei266 – 2661SubstrateUniRule annotation
    Binding sitei294 – 2941Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei479 – 4791Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei575 – 5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei638 – 6381Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei664 – 6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei745 – 7451Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi90 – 912ATPUniRule annotation
    Nucleotide bindingi120 – 1234ATPUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    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

    SABIO-RKQ27778.
    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:PFK
    OrganismiSchistosoma mansoni (Blood fluke)
    Taxonomic identifieri6183 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 781781ATP-dependent 6-phosphofructokinasePRO_0000112033Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi6183.Smp_043670.2__mRNA.

    Structurei

    3D structure databases

    ProteinModelPortaliQ27778.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 394394N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni166 – 1683Substrate bindingUniRule annotation
    Regioni210 – 2123Substrate bindingUniRule annotation
    Regioni300 – 3034Substrate bindingUniRule annotation
    Regioni395 – 40915Interdomain linkerAdd
    BLAST
    Regioni410 – 781372C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni537 – 5415Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni582 – 5843Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni670 – 6734Allosteric 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

    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. 2 hits.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q27778-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATWMEGKYV ARGQFTGECI AVLTSGGDAQ GMNAAVRAVV RMGIYCGCRV
    60 70 80 90 100
    FFIREGYQGL VDGGQNIQEA SWADVSGILQ LGGTKIGSAR CMDFRERYGR
    110 120 130 140 150
    LKAAENLVKN QITNLVVIGG DGSLTGANLF RAEWSSLLEE LVTSNKISAE
    160 170 180 190 200
    SAKQFHRLNI VGLVGSIDND FCGTDMTIGA DSALHRIIEA TDAISTTAHS
    210 220 230 240 250
    HQRCFILEVM GRHCGYLALV ASMACEADWV FIPEMPPTDD WREKLCHKLR
    260 270 280 290 300
    MNREHGQRVN IIMVAEGAID RACKPITCEI VKNLIVSELQ LDTRITVLGH
    310 320 330 340 350
    VQRGGSPSAF DRILGSRMGA EAVLALMDAD RDPNLPSCVI SLDGNQAVRV
    360 370 380 390 400
    PLVKCVDRTR QVAEAMKACD FDHAVELRGT SFMNNLATYI KLSKIEQPRQ
    410 420 430 440 450
    SVMSSENNLR IGIVNVGAPA CGINAVIRGF TRLGITKGYK VIGIHEGFSG
    460 470 480 490 500
    LVKGDASEIQ WADVRGWVGM GGSMLGTRRD TPNGLGIDKV AAKFKELKLS
    510 520 530 540 550
    GLLIIGGFEA YECMIELVEG REKYPELCIP MAMVPATISN NVPGTDFSLG
    560 570 580 590 600
    CDTALNEITS VLDKIKQSAL GTKRRVFVVE TMGGYCGYLA TMSALAGGAD
    610 620 630 640 650
    AAYIFEEPFT IDDLREDVVH LRAKIDDNVK RGLVLRADML INTITSEFIH
    660 670 680 690 700
    QLYAQEGQGI FDCRCNVLGH MQQGDRPSPF DRSLGTKFAS KAIDWLDEQI
    710 720 730 740 750
    NANIVQILQS IHQTFMLYIN WYCTSSDNLF KYSLELREHT DFVHRLPKEE
    760 770 780
    WWLSLRPLMR IMAKHDSLYE SESIMAGTDR K
    Length:781
    Mass (Da):86,060
    Last modified:November 1, 1996 - v1
    Checksum:iB2CDF20CAE926C38
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L31531 mRNA. Translation: AAA29911.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L31531 mRNA. Translation: AAA29911.1.

    3D structure databases

    ProteinModelPortaliQ27778.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi6183.Smp_043670.2__mRNA.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    SABIO-RKQ27778.

    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. 2 hits.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning and characterization of a cDNA encoding phosphofructokinase from Schistosoma mansoni."
      Ding J., Su J.G.J., Mansour T.E.
      Mol. Biochem. Parasitol. 66:105-110(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
    2. "Purification, kinetics and inhibition by antimonials of recombinant phosphofructokinase from Schistosoma mansoni."
      Su J.G., Mansour J.M., Mansour T.E.
      Mol. Biochem. Parasitol. 81:171-178(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

    Entry informationi

    Entry nameiPFKA_SCHMA
    AccessioniPrimary (citable) accession number: Q27778
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: June 24, 2015
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. 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.