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Q9WY52

- PFKA_THEMA

UniProt

Q9WY52 - PFKA_THEMA

Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. Can partially be replaced by manganese and iron.1 PublicationUniRule annotation

    Enzyme regulationi

    Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. Strongly inhibited by diphosphate, triphosphate and polyphosphate.1 PublicationUniRule annotation

    Kineticsi

    1. KM=0.2 mM for ATP (at 75 degrees Celsius)2 Publications
    2. KM=7.6 mM for fructose 1,6-bisphosphate (at 75 degrees Celsius)2 Publications
    3. KM=1.4 mM for ADP (at 75 degrees Celsius)2 Publications

    Vmax=360 µmol/min/mg enzyme for the forward reaction (at 75 degrees Celsius)2 Publications

    Vmax=432 µmol/min/mg enzyme for the forward reaction (at 50 degrees Celsius)2 Publications

    Vmax=13 µmol/min/mg enzyme for the reverse reaction (at 75 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 6.7.2 Publications

    Temperature dependencei

    Optimum temperature is 93 degrees Celsius.2 Publications

    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 sitei244 – 2441Substrate; 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

    BioCyciMetaCyc:MONOMER-363.
    SABIO-RKQ9WY52.
    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:pfkAUniRule annotation
    Ordered Locus Names:TM_0209
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: 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 – 319319ATP-dependent 6-phosphofructokinasePRO_0000112000Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi243274.TM0209.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WY52.
    SMRiQ9WY52. Positions 1-319.
    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
    Regioni250 – 2534Substrate 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.
    KOiK00850.
    OMAiGFGGRCV.
    OrthoDBiEOG644ZRM.

    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.

    Q9WY52-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKIAVLTSG GDAPGMNAAV RAVVRYGVRQ GLEVIGVRRG YSGLIDGDFV    50
    KLEYKDVAGI TEKGGTILRT SRCEEFKTEE GRELAAKQIK KHGIEGLVVI 100
    GGEGSLTGAH LLYEEHKIPV VGIPATIDND IGLTDMCIGV DTCLNTVMDA 150
    VQKLKDTASS HERAFIVEVM GRHSGYIALM AGLVTGAEAI IVPEIPVDYS 200
    QLADRILEER RRGKINSIII VAEGAASAYT VARHLEYRIG YETRITILGH 250
    VQRGGSPTAF DRRLALSMGV EAVDALLDGE VDVMIALQGN KFVRVPIMEA 300
    LSTKKTIDKK LYEIAHMLS 319
    Length:319
    Mass (Da):34,487
    Last modified:November 1, 1999 - v1
    Checksum:i3809E971288D12B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21K → R AA sequence (PubMed:11976749)Curated
    Sequence conflicti14 – 174PGMN → GPM AA sequence (PubMed:11976749)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35301.1.
    PIRiC72406.
    RefSeqiNP_228024.1. NC_000853.1.
    YP_007976558.1. NC_021214.1.
    YP_008990817.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35301; AAD35301; TM_0209.
    GeneIDi897081.
    KEGGitma:TM0209.
    tmi:THEMA_03680.
    tmm:Tmari_0207.
    PATRICi23935290. VBITheMar51294_0211.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35301.1 .
    PIRi C72406.
    RefSeqi NP_228024.1. NC_000853.1.
    YP_007976558.1. NC_021214.1.
    YP_008990817.1. NC_023151.1.

    3D structure databases

    ProteinModelPortali Q9WY52.
    SMRi Q9WY52. Positions 1-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM0209.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD35301 ; AAD35301 ; TM_0209 .
    GeneIDi 897081.
    KEGGi tma:TM0209.
    tmi:THEMA_03680.
    tmm:Tmari_0207.
    PATRICi 23935290. VBITheMar51294_0211.

    Phylogenomic databases

    eggNOGi COG0205.
    KOi K00850.
    OMAi GFGGRCV.
    OrthoDBi EOG644ZRM.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BioCyci MetaCyc:MONOMER-363.
    SABIO-RK Q9WY52.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "ATP-dependent 6-phosphofructokinase from the hyperthermophilic bacterium Thermotoga maritima: characterization of an extremely thermophilic, allosterically regulated enzyme."
      Hansen T., Musfeldt M., Schonheit P.
      Arch. Microbiol. 177:401-409(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-39, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION.
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes."
      Ding Y.R., Ronimus R.S., Morgan H.W.
      J. Bacteriol. 183:791-794(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

    Entry informationi

    Entry nameiPFKA_THEMA
    AccessioniPrimary (citable) accession number: Q9WY52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 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