Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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 annotation1 Publication

Enzyme regulationi

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.UniRule annotation1 Publication2 Publications

Kineticsi

  1. KM=0.07 mM for ATP1 Publication
  2. KM=0.033 mM for fructose 6-phosphate1 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. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase B (pgiB), Glucose-6-phosphate isomerase A (pgiA), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgiB)
    3. ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA)
    4. Fructose-bisphosphate aldolase (fba)
    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)DescriptionActionsGraphical viewLength
    Binding sitei11ATP; via amide nitrogenUniRule annotation1
    Binding sitei59Allosteric activator ADP; shared with dimeric partnerUniRule annotation1 Publication1
    Metal bindingi103Magnesium; catalyticUniRule annotation1 Publication1
    Active sitei127Proton acceptorUniRule annotation1
    Binding sitei154Allosteric activator ADPUniRule annotation1 Publication1
    Binding sitei162Substrate; shared with dimeric partnerUniRule annotation1 Publication1
    Binding sitei211Allosteric activator ADPUniRule annotation1 Publication1
    Binding sitei222SubstrateUniRule annotation2 Publications1
    Binding sitei243Substrate; shared with dimeric partnerUniRule annotation2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi72 – 73ATPUniRule annotation1 Publication2
    Nucleotide bindingi102 – 105ATPUniRule annotation4

    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

    BRENDAi2.7.1.11. 623.
    SABIO-RKP00512.
    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
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001119351 – 319ATP-dependent 6-phosphofructokinaseAdd BLAST319

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation4 Publications

    Structurei

    Secondary structure

    1319
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 11Combined sources9
    Helixi16 – 29Combined sources14
    Beta strandi33 – 37Combined sources5
    Helixi40 – 46Combined sources7
    Beta strandi49 – 52Combined sources4
    Helixi54 – 57Combined sources4
    Helixi74 – 77Combined sources4
    Helixi81 – 91Combined sources11
    Beta strandi97 – 102Combined sources6
    Helixi103 – 114Combined sources12
    Beta strandi119 – 127Combined sources9
    Helixi139 – 153Combined sources15
    Beta strandi159 – 168Combined sources10
    Helixi175 – 183Combined sources9
    Beta strandi187 – 190Combined sources4
    Helixi198 – 210Combined sources13
    Beta strandi216 – 221Combined sources6
    Turni222 – 224Combined sources3
    Helixi227 – 238Combined sources12
    Beta strandi241 – 246Combined sources6
    Helixi248 – 252Combined sources5
    Helixi258 – 277Combined sources20
    Beta strandi281 – 287Combined sources7
    Beta strandi290 – 295Combined sources6
    Helixi296 – 300Combined sources5
    Helixi308 – 317Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MTOX-ray3.20A/B/C/D/E/F/G/H1-319[»]
    3PFKX-ray2.40A1-319[»]
    3U39X-ray2.79A/B/C/D1-319[»]
    4I36X-ray2.30A/B/C/D1-319[»]
    4I4IX-ray2.49A/B/C/D1-319[»]
    4I7EX-ray2.00A/B/C/D1-319[»]
    4PFKX-ray2.40A1-319[»]
    6PFKX-ray2.60A/B/C/D1-319[»]
    ProteinModelPortaliP00512.
    SMRiP00512.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00512.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni21 – 25Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation1 Publication5
    Regioni125 – 127Substrate bindingUniRule annotation2 Publications3
    Regioni169 – 171Substrate bindingUniRule annotation2 Publications3
    Regioni185 – 187Allosteric activator ADP bindingUniRule annotation1 Publication3
    Regioni213 – 215Allosteric activator ADP bindingUniRule annotation1 Publication3
    Regioni249 – 252Substrate bindingUniRule annotation2 Publications4

    Sequence similaritiesi

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

    Family and domain databases

    CDDicd00763. Bacterial_PFK. 1 hit.
    HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
    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.

    P00512-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKRIGVLTSG GDSPGMNAAI RSVVRKAIYH GVEVYGVYHG YAGLIAGNIK
    60 70 80 90 100
    KLEVGDVGDI IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI
    110 120 130 140 150
    GGDGSYQGAK KLTEHGFPCV GVPGTIDNDI PGTDFTIGFD TALNTVIDAI
    160 170 180 190 200
    DKIRDTATSH ERTYVIEVMG RHAGDIALWS GLAGGAETIL IPEADYDMND
    210 220 230 240 250
    VIARLKRGHE RGKKHSIIIV AEGVGSGVDF GRQIQEATGF ETRVTVLGHV
    260 270 280 290 300
    QRGGSPTAFD RVLASRLGAR AVELLLEGKG GRCVGIQNNQ LVDHDIAEAL
    310
    ANKHTIDQRM YALSKELSI
    Length:319
    Mass (Da):34,119
    Last modified:July 1, 1989 - v2
    Checksum:iEE968D39BA30712B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti12D → N AA sequence (PubMed:6447595).Curated1
    Sequence conflicti35 – 37Missing AA sequence (PubMed:6447595).Curated3
    Sequence conflicti43G → V AA sequence (PubMed:6447595).Curated1
    Sequence conflicti82Q → E AA sequence (PubMed:6447595).Curated1
    Sequence conflicti95E → Q AA sequence (PubMed:6447595).Curated1
    Sequence conflicti225G → L AA sequence (PubMed:6447595).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M15643 Genomic DNA. Translation: AAA22656.1.
    D13095 Genomic DNA. Translation: BAA02405.1.
    PIRiA27474. KIBSFF.
    RefSeqiWP_033014452.1. NZ_LUCR01000070.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M15643 Genomic DNA. Translation: AAA22656.1.
    D13095 Genomic DNA. Translation: BAA02405.1.
    PIRiA27474. KIBSFF.
    RefSeqiWP_033014452.1. NZ_LUCR01000070.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MTOX-ray3.20A/B/C/D/E/F/G/H1-319[»]
    3PFKX-ray2.40A1-319[»]
    3U39X-ray2.79A/B/C/D1-319[»]
    4I36X-ray2.30A/B/C/D1-319[»]
    4I4IX-ray2.49A/B/C/D1-319[»]
    4I7EX-ray2.00A/B/C/D1-319[»]
    4PFKX-ray2.40A1-319[»]
    6PFKX-ray2.60A/B/C/D1-319[»]
    ProteinModelPortaliP00512.
    SMRiP00512.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.
    BRENDAi2.7.1.11. 623.
    SABIO-RKP00512.

    Miscellaneous databases

    EvolutionaryTraceiP00512.

    Family and domain databases

    CDDicd00763. Bacterial_PFK. 1 hit.
    HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
    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...

    Entry informationi

    Entry nameiPFKA_GEOSE
    AccessioniPrimary (citable) accession number: P00512
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: November 30, 2016
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In the R state the 6-P group of fructose 6-phosphate (F6P) is bound by His-249 from one chain and Arg-162 and Arg-243 from an adjacent chain. In the T state a conformation change moves Arg-162 away from the substrate. Glu-161 takes its place, hence repelling the phosphate of ATP.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.