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Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene
N/A
Organism
Naegleria fowleri (Brain eating amoeba)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation1 Publication, Mn2+UniRule annotation1 Publication

Enzyme regulationi

Activated by AMP. Probably promotes oligomerization of the enzyme.1 Publication

Kineticsi

  1. KM=590 µM for phosphate1 Publication
  2. KM=15 µM for diphosphate1 Publication
  3. KM=10 µM for fructose 6-phosphate1 Publication
  4. KM=35 µM for fructose 1,6-bisphosphate1 Publication

    pH dependencei

    Optimum pH is 6 for the forward reaction and 7.5 for the reverse reaction.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. no protein annotated in this organism
    3. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
    4. no protein annotated in this organism
    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 – 271Diphosphate; via amide nitrogenUniRule annotation
    Metal bindingi122 – 1221Magnesium; catalyticUniRule annotation
    Sitei123 – 1231Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATPUniRule annotation
    Sitei146 – 1461Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation
    Active sitei149 – 1491Proton acceptorUniRule annotation
    Binding sitei261 – 2611SubstrateUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferaseUniRule annotation (EC:2.7.1.90UniRule annotation)
    Alternative name(s):
    6-phosphofructokinase, pyrophosphate dependentUniRule annotation
    PPi-dependent phosphofructokinaseUniRule annotation
    Short name:
    PPi-PFKUniRule annotation
    Pyrophosphate-dependent 6-phosphofructose-1-kinaseUniRule annotation
    OrganismiNaegleria fowleri (Brain eating amoeba)
    Taxonomic identifieri5763 [NCBI]
    Taxonomic lineageiEukaryotaHeteroloboseaSchizopyrenidaVahlkampfiidaeNaegleria

    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 – 437437Pyrophosphate--fructose 6-phosphate 1-phosphotransferasePRO_0000429701Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ27705.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni147 – 1493Substrate bindingUniRule annotation
    Regioni193 – 1953Substrate bindingUniRule annotation
    Regioni323 – 3264Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade "Short" sub-subfamily.UniRule annotation

    Family and domain databases

    HAMAPiMF_01979. Phosphofructokinase_II_Short. 1 hit.
    InterProiIPR022953. ATP_PFK.
    IPR000023. Phosphofructokinase_dom.
    IPR011403. PPi-PFK_TM0289.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036482. PPi_PFK_TM0289. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q27705-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLSSSHLPTT IVTPKNVPTL GVLVGGGPAP GINGVIGAVT IEAINNGYRV
    60 70 80 90 100
    LGFLEGFQNL ILQDDSKIVE LTIDSVSRIH FEGGSILKTS RANPTKKQED
    110 120 130 140 150
    LQKVVKQLQK FNVSLLVTIG GDDTAFSSMS VAKAANNEIH VVTLPKTIDN
    160 170 180 190 200
    DLPLPYGIPT FGYETAREFG ANVVRNLMTD ASTASRYFIV VAMGRQAGHL
    210 220 230 240 250
    ALGIGKSAGS HLTLIPEEFL PTTDSTEPEV TFSRICDMIE ASIIKRLYTS
    260 270 280 290 300
    KKDHGVIVLA EGLLEYMSTD ELKQAFGSSL KYDAHDHIML AELDFGRLVR
    310 320 330 340 350
    DEMRERMNRR GLKIAFTEKN LGYELRCAPP NAFDREYTRD LGNGAVRYLL
    360 370 380 390 400
    NGGNGALITV QGVKMVPLSF DDLKDPRTGK TRTRQVDVSS EGFQVAKRYM
    410 420 430
    IRLEKKDFEK EETLKGLAAT AKCSVEDFIK QFKYLVQ
    Length:437
    Mass (Da):48,098
    Last modified:November 1, 1996 - v1
    Checksum:i20863E055F18A284
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U11733 mRNA. Translation: AAA85791.1.
    PIRiS54978.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U11733 mRNA. Translation: AAA85791.1.
    PIRiS54978.

    3D structure databases

    ProteinModelPortaliQ27705.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.

    Family and domain databases

    HAMAPiMF_01979. Phosphofructokinase_II_Short. 1 hit.
    InterProiIPR022953. ATP_PFK.
    IPR000023. Phosphofructokinase_dom.
    IPR011403. PPi-PFK_TM0289.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036482. PPi_PFK_TM0289. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPFP_NAEFO
    AccessioniPrimary (citable) accession number: Q27705
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: November 1, 1996
    Last modified: September 7, 2016
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    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.