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Protein

ATP-dependent 6-phosphofructokinase 1

Gene

pfkA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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 annotation2 Publications

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 and other diphosphonucleosides (By similarity). Allosterically inhibited by phosphoenolpyruvate which induces the dissociation of the active tetramer into an inactive two-subunit forms.By similarity1 Publication

Kineticsi

  1. KM=0.08 mM for ATP1 Publication
  2. KM=0.025 mM for fructose 6-phosphate1 Publication

    pH dependencei

    Optimum pH is 8.4.1 Publication

    Temperature dependencei

    Optimum temperature is 85 degrees Celsius.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 (pgi)
    3. ATP-dependent 6-phosphofructokinase 2 (pfkA2), ATP-dependent 6-phosphofructokinase 1 (pfkA)
    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 sitei11 – 111ATP; via amide nitrogenUniRule annotation
    Metal bindingi103 – 1031Magnesium; catalyticUniRule annotation
    Active sitei128 – 1281Proton acceptorUniRule annotation
    Binding sitei155 – 1551Allosteric activator ADPUniRule annotation
    Binding sitei163 – 1631Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei212 – 2121Allosteric activator ADPUniRule annotation
    Binding sitei223 – 2231SubstrateUniRule annotation
    Binding sitei246 – 2461Substrate; shared with dimeric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi72 – 732ATPUniRule annotation
    Nucleotide bindingi102 – 1054ATPUniRule 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

    BioCyciTTHE300852:GH8R-2012-MONOMER.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase 1UniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFK 1UniRule annotation
    Short name:
    Phosphofructokinase 1UniRule annotation
    Alternative name(s):
    Phosphohexokinase 1UniRule annotation
    Gene namesi
    Name:pfkAUniRule annotation
    Ordered Locus Names:TTHA1962
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532 Componenti: Chromosome

    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 – 322322ATP-dependent 6-phosphofructokinase 1PRO_0000112001Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi300852.TTHA1962.

    Structurei

    3D structure databases

    ProteinModelPortaliP21777.
    SMRiP21777. Positions 1-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 255Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation
    Regioni126 – 1283Substrate bindingUniRule annotation
    Regioni170 – 1723Substrate bindingUniRule annotation
    Regioni186 – 1883Allosteric activator ADP bindingUniRule annotation
    Regioni214 – 2163Allosteric activator ADP bindingUniRule annotation
    Regioni252 – 2554Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0205.
    HOGENOMiHOG000248869.
    KOiK00850.
    OMAiISKMESH.
    OrthoDBiEOG644ZRM.
    PhylomeDBiP21777.

    Family and domain databases

    HAMAPiMF_00339. Phosphofructokinase_I_B1.
    InterProiIPR022953. ATP_PFK.
    IPR012003. ATP_PFK_prok-type.
    IPR012828. PFKA_ATP_prok.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.
    TIGRFAMsiTIGR02482. PFKA_ATP. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21777-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKRIGVFTSG GDAPGMNAAI RAVVRQAHAL GVEVIGIRRG YAGMIQGEMV
    60 70 80 90 100
    PLGVRDVANI IQRGGTILLT ARSQEFLTEE GRAKAYAKLQ AAGIEGLVAI
    110 120 130 140 150
    GGDGTFRGAL CLVEEHGMPV VGVPGTIDND LYGTDYTIGF DTAVNTALEA
    160 170 180 190 200
    IDRIRDTAAS HERVFFIEVM GRHAGFIALD VGLAGGAEVI AVPEEPVDPK
    210 220 230 240 250
    AVAEVLEASQ RRGKKSSIVV VAEGAYPGGA AGLLAAIREH LQVEARVTVL
    260 270 280 290 300
    GHIQRGGSPT AKDRILASRL GAAAVEALVG GASGVMVGEV EGEVDLTPLK
    310 320
    EAVERRKDIN RALLRLSQVL AL
    Length:322
    Mass (Da):33,537
    Last modified:March 29, 2005 - v3
    Checksum:i608CD4053E6ACEA3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111C → F in AAA27501 (PubMed:1828151).Curated
    Sequence conflicti273 – 2731A → P in AAA27501 (PubMed:1828151).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M71213 Genomic DNA. Translation: AAA27501.1.
    AP008226 Genomic DNA. Translation: BAD71785.1.
    RefSeqiWP_011173968.1. NC_006461.1.
    YP_145228.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD71785; BAD71785; BAD71785.
    GeneIDi3169721.
    KEGGittj:TTHA1962.
    PATRICi23958903. VBITheThe93045_1933.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M71213 Genomic DNA. Translation: AAA27501.1.
    AP008226 Genomic DNA. Translation: BAD71785.1.
    RefSeqiWP_011173968.1. NC_006461.1.
    YP_145228.1. NC_006461.1.

    3D structure databases

    ProteinModelPortaliP21777.
    SMRiP21777. Positions 1-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi300852.TTHA1962.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD71785; BAD71785; BAD71785.
    GeneIDi3169721.
    KEGGittj:TTHA1962.
    PATRICi23958903. VBITheThe93045_1933.

    Phylogenomic databases

    eggNOGiCOG0205.
    HOGENOMiHOG000248869.
    KOiK00850.
    OMAiISKMESH.
    OrthoDBiEOG644ZRM.
    PhylomeDBiP21777.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    BioCyciTTHE300852:GH8R-2012-MONOMER.

    Family and domain databases

    HAMAPiMF_00339. Phosphofructokinase_I_B1.
    InterProiIPR022953. ATP_PFK.
    IPR012003. ATP_PFK_prok-type.
    IPR012828. PFKA_ATP_prok.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.
    TIGRFAMsiTIGR02482. PFKA_ATP. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning of phosphofructokinase 1 gene from a thermophilic bacterium, Thermus thermophilus."
      Xu J., Seki M., Denda K., Yoshida M.
      Biochem. Biophys. Res. Commun. 176:1313-1318(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    3. "Phosphoenolpyruvate-insensitive phosphofructokinase isozyme from Thermus thermophilus HB8."
      Xu J., Oshima T., Yoshida M.
      J. Biochem. 109:199-203(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-25.
    4. "Allosteric nature of thermostable phosphofructokinase from an extreme thermophilic bacterium."
      Yoshida M.
      Biochemistry 11:1087-1093(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: HB8 / ATCC 27634 / DSM 579.
    5. "Tetramer-dimer conversion of phosphofructokinase from Thermus thermophilus induced by its allosteric effectors."
      Xu J., Oshima T., Yoshida M.
      J. Mol. Biol. 215:597-606(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
      Strain: HB8 / ATCC 27634 / DSM 579.

    Entry informationi

    Entry nameiPFKA1_THET8
    AccessioniPrimary (citable) accession number: P21777
    Secondary accession number(s): Q5SGW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: March 29, 2005
    Last modified: May 27, 2015
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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. 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.