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P21777

- PFKA1_THET8

UniProt

P21777 - PFKA1_THET8

Protein

ATP-dependent 6-phosphofructokinase 1

Gene

pfkA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.2 PublicationsUniRule annotation

    Catalytic activityi

    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.2 PublicationsUniRule annotation

    Cofactori

    Magnesium.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

    Pathwayi

    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

    1. 6-phosphofructokinase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. fructose 6-phosphate metabolic process Source: InterPro
    2. glycolytic process Source: UniProtKB-HAMAP

    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: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro

    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.1 PublicationUniRule annotation

    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.
    OMAiYRRGKLH.
    OrthoDBiEOG644ZRM.
    PhylomeDBiP21777.

    Family and domain databases

    HAMAPiMF_00339. Phosphofructokinase_I_B1.
    InterProiIPR012003. ATP_PFK_prok.
    IPR012828. PFKA_ATP.
    IPR022953. Phosphofructokinase.
    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

    MKRIGVFTSG GDAPGMNAAI RAVVRQAHAL GVEVIGIRRG YAGMIQGEMV    50
    PLGVRDVANI IQRGGTILLT ARSQEFLTEE GRAKAYAKLQ AAGIEGLVAI 100
    GGDGTFRGAL CLVEEHGMPV VGVPGTIDND LYGTDYTIGF DTAVNTALEA 150
    IDRIRDTAAS HERVFFIEVM GRHAGFIALD VGLAGGAEVI AVPEEPVDPK 200
    AVAEVLEASQ RRGKKSSIVV VAEGAYPGGA AGLLAAIREH LQVEARVTVL 250
    GHIQRGGSPT AKDRILASRL GAAAVEALVG GASGVMVGEV EGEVDLTPLK 300
    EAVERRKDIN RALLRLSQVL AL 322
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M71213 Genomic DNA. Translation: AAA27501.1.
    AP008226 Genomic DNA. Translation: BAD71785.1.
    RefSeqiYP_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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M71213 Genomic DNA. Translation: AAA27501.1 .
    AP008226 Genomic DNA. Translation: BAD71785.1 .
    RefSeqi YP_145228.1. NC_006461.1.

    3D structure databases

    ProteinModelPortali P21777.
    SMRi P21777. Positions 1-321.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA1962.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD71785 ; BAD71785 ; BAD71785 .
    GeneIDi 3169721.
    KEGGi ttj:TTHA1962.
    PATRICi 23958903. VBITheThe93045_1933.

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000248869.
    KOi K00850.
    OMAi YRRGKLH.
    OrthoDBi EOG644ZRM.
    PhylomeDBi P21777.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BioCyci TTHE300852:GH8R-2012-MONOMER.

    Family and domain databases

    HAMAPi MF_00339. Phosphofructokinase_I_B1.
    InterProi IPR012003. ATP_PFK_prok.
    IPR012828. PFKA_ATP.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view ]
    Pfami PF00365. PFK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000532. ATP_PFK_prok. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 1 hit.
    TIGRFAMsi TIGR02482. PFKA_ATP. 1 hit.
    PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 108 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