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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
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 annotation1 Publication

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.UniRule annotation

Kineticsi

  1. KM=0.18 mM for ATP1 Publication
  2. KM=0.25 mM for fructose 6-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.2-7.8.1 Publication

    Pathway:iglycolysis

    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 (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 sitei127 – 1271Proton acceptorUniRule annotation
    Binding sitei154 – 1541Allosteric activator ADPUniRule annotation
    Binding sitei162 – 1621Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei211 – 2111Allosteric activator ADPUniRule annotation
    Binding sitei222 – 2221SubstrateUniRule 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

    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

    BioCyciLLAC272623:GHSH-1422-MONOMER.
    MetaCyc:MONOMER-13044.
    SABIO-RKQ07636.
    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
    Synonyms:pfk
    Ordered Locus Names:LL1333
    ORF Names:L0002
    OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
    Taxonomic identifieri272623 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    ProteomesiUP000002196 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 – 340340ATP-dependent 6-phosphofructokinasePRO_0000111958Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi272623.L0002.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07636.
    SMRiQ07636. Positions 1-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 255Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation
    Regioni125 – 1273Substrate bindingUniRule annotation
    Regioni169 – 1713Substrate bindingUniRule annotation
    Regioni185 – 1873Allosteric activator ADP bindingUniRule annotation
    Regioni213 – 2153Allosteric 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.
    HOGENOMiHOG000248870.
    KOiK00850.
    OMAiGFGGRCV.
    OrthoDBiEOG644ZRM.

    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.

    Q07636-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKRIAVLTSG GDAPGMNAAI RAVVRKAISE GIEVYGINHG YAGMVAGDIF
    60 70 80 90 100
    PLTSASVGDK IGRGGTFLYS ARYPEFAQVE GQLAGIEQLK KFGIEGVVVI
    110 120 130 140 150
    GGDGSYHGAM RLTEHGFPAV GLPGTIDNDI VGTDFTIGFD TAVSTVVDAL
    160 170 180 190 200
    DKIRDTSSSH NRTFVVEVMG RNAGDIALNA GIAAGADDIC IPEKEFKFEN
    210 220 230 240 250
    VVNNINKGYE KGKNHHIIVL AEGVMTGEEF ATKLKEAGYK GDLRVSVLGH
    260 270 280 290 300
    IQRGGSPTAR DRVLASRMGA RAVELLRDGI GGVAVGIRNE ELVESPILGT
    310 320 330 340
    AEEGALFSLT TEGGIKVNNP HKAGLELYRL NSALNNLNLN
    Length:340
    Mass (Da):35,806
    Last modified:October 1, 1994 - v1
    Checksum:iF1BB2BD3FD3661B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901C → S AA sequence (PubMed:8333872).Curated
    Sequence conflicti194 – 1941K → L AA sequence (PubMed:8333872).Curated
    Sequence conflicti219 – 2202VL → IV AA sequence (PubMed:8333872).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L07920 Genomic DNA. Translation: AAA99894.1.
    AE005176 Genomic DNA. Translation: AAK05431.1.
    PIRiA40620. JN0614.
    RefSeqiNP_267489.1. NC_002662.1.
    WP_003131080.1. NC_002662.1.

    Genome annotation databases

    EnsemblBacteriaiAAK05431; AAK05431; L0002.
    GeneIDi1114983.
    KEGGilla:L0002.
    PATRICi22295064. VBILacLac136773_1440.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L07920 Genomic DNA. Translation: AAA99894.1.
    AE005176 Genomic DNA. Translation: AAK05431.1.
    PIRiA40620. JN0614.
    RefSeqiNP_267489.1. NC_002662.1.
    WP_003131080.1. NC_002662.1.

    3D structure databases

    ProteinModelPortaliQ07636.
    SMRiQ07636. Positions 1-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272623.L0002.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK05431; AAK05431; L0002.
    GeneIDi1114983.
    KEGGilla:L0002.
    PATRICi22295064. VBILacLac136773_1440.

    Phylogenomic databases

    eggNOGiCOG0205.
    HOGENOMiHOG000248870.
    KOiK00850.
    OMAiGFGGRCV.
    OrthoDBiEOG644ZRM.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    BioCyciLLAC272623:GHSH-1422-MONOMER.
    MetaCyc:MONOMER-13044.
    SABIO-RKQ07636.

    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. "The primary structure of phosphofructokinase from Lactococcus lactis."
      Xiao Q., Moore C.H.
      Biochem. Biophys. Res. Commun. 194:65-71(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: C10.
    2. "Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: phosphofructokinase, pyruvate kinase, and lactate dehydrogenase."
      Llanos R.M., Harris C.J., Hillier A.J., Davidson B.E.
      J. Bacteriol. 175:2541-2551(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LM0230.
    3. "The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
      Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
      Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: IL1403.
    4. "Phosphofructokinase from Streptococcus lactis."
      Fordyce A.M., Moore C.H., Pritchard G.G.
      Methods Enzymol. 90:77-82(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiPFKA_LACLA
    AccessioniPrimary (citable) accession number: Q07636
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: July 22, 2015
    This is version 114 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

    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.