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P00512

- PFKA_GEOSE

UniProt

P00512 - PFKA_GEOSE

Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      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.1 PublicationUniRule annotation

    Catalytic activityi

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

    Cofactori

    Magnesium.UniRule annotation

    Enzyme regulationi

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

    Kineticsi

    1. KM=0.07 mM for ATP1 Publication
    2. KM=0.033 mM for fructose 6-phosphate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111ATP; via amide nitrogen
    Binding sitei59 – 591Allosteric activator ADP; shared with dimeric partner
    Metal bindingi103 – 1031Magnesium; catalyticUniRule annotation
    Active sitei127 – 1271Proton acceptor
    Binding sitei154 – 1541Allosteric activator ADP
    Binding sitei162 – 1621Substrate; shared with dimeric partner
    Binding sitei211 – 2111Allosteric activator ADP
    Binding sitei222 – 2221Substrate
    Binding sitei243 – 2431Substrate; shared with dimeric partner

    Regions

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

    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

    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

    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_0000111935Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.4 PublicationsUniRule annotation

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Helixi16 – 2914
    Beta strandi33 – 375
    Helixi40 – 467
    Beta strandi49 – 524
    Helixi54 – 574
    Helixi74 – 774
    Helixi81 – 9111
    Beta strandi97 – 1026
    Helixi103 – 11412
    Beta strandi119 – 1279
    Helixi139 – 15315
    Beta strandi159 – 16810
    Helixi175 – 1839
    Beta strandi187 – 1904
    Helixi198 – 21013
    Beta strandi216 – 2216
    Turni222 – 2243
    Helixi227 – 23812
    Beta strandi241 – 2466
    Helixi248 – 2525
    Helixi258 – 27720
    Beta strandi281 – 2877
    Beta strandi290 – 2956
    Helixi296 – 3005
    Helixi308 – 31710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 1-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00512.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 255Allosteric activator ADP binding; shared with dimeric partner
    Regioni125 – 1273Substrate binding
    Regioni169 – 1713Substrate binding
    Regioni185 – 1873Allosteric activator ADP binding
    Regioni213 – 2153Allosteric activator ADP binding
    Regioni249 – 2524Substrate binding

    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

    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.

    P00512-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRIGVLTSG GDSPGMNAAI RSVVRKAIYH GVEVYGVYHG YAGLIAGNIK    50
    KLEVGDVGDI IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI 100
    GGDGSYQGAK KLTEHGFPCV GVPGTIDNDI PGTDFTIGFD TALNTVIDAI 150
    DKIRDTATSH ERTYVIEVMG RHAGDIALWS GLAGGAETIL IPEADYDMND 200
    VIARLKRGHE RGKKHSIIIV AEGVGSGVDF GRQIQEATGF ETRVTVLGHV 250
    QRGGSPTAFD RVLASRLGAR AVELLLEGKG GRCVGIQNNQ LVDHDIAEAL 300
    ANKHTIDQRM YALSKELSI 319
    Length:319
    Mass (Da):34,119
    Last modified:July 1, 1989 - v2
    Checksum:iEE968D39BA30712B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121D → N AA sequence (PubMed:6447595)Curated
    Sequence conflicti35 – 373Missing AA sequence (PubMed:6447595)Curated
    Sequence conflicti43 – 431G → V AA sequence (PubMed:6447595)Curated
    Sequence conflicti82 – 821Q → E AA sequence (PubMed:6447595)Curated
    Sequence conflicti95 – 951E → Q AA sequence (PubMed:6447595)Curated
    Sequence conflicti225 – 2251G → L AA sequence (PubMed:6447595)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15643 Genomic DNA. Translation: AAA22656.1.
    D13095 Genomic DNA. Translation: BAA02405.1.
    PIRiA27474. KIBSFF.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15643 Genomic DNA. Translation: AAA22656.1 .
    D13095 Genomic DNA. Translation: BAA02405.1 .
    PIRi A27474. KIBSFF.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MTO X-ray 3.20 A/B/C/D/E/F/G/H 1-319 [» ]
    3PFK X-ray 2.40 A 1-319 [» ]
    3U39 X-ray 2.79 A/B/C/D 1-319 [» ]
    4I36 X-ray 2.30 A/B/C/D 1-319 [» ]
    4I4I X-ray 2.49 A/B/C/D 1-319 [» ]
    4I7E X-ray 2.00 A/B/C/D 1-319 [» ]
    4PFK X-ray 2.40 A 1-319 [» ]
    6PFK X-ray 2.60 A/B/C/D 1-319 [» ]
    ProteinModelPortali P00512.
    SMRi P00512. Positions 1-319.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    SABIO-RK P00512.

    Miscellaneous databases

    EvolutionaryTracei P00512.

    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. "Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene."
      French B.A., Chang S.H.
      Gene 54:65-71(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus."
      Kolb E., Hudson P.J., Harris J.I.
      Eur. J. Biochem. 108:587-597(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    3. "Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon."
      Sakai H., Ohta T.
      Eur. J. Biochem. 211:851-859(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-319.
    4. "Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme."
      Byrnes M., Zhu X., Younathan E.S., Chang S.H.
      Biochemistry 33:3424-3431(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Structure and control of phosphofructokinase from Bacillus stearothermophilus."
      Evans P.R., Hudson P.J.
      Nature 279:500-504(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    6. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP AND FRUCTOSE-6-PHOSPHATE.
    7. "Structural basis of the allosteric behaviour of phosphofructokinase."
      Schirmer T., Evans P.R.
      Nature 343:140-145(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC INHIBITOR.
    8. "Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus."
      Riley-Lovingshimer M.R., Ronning D.R., Sacchettini J.C., Reinhart G.D.
      Biochemistry 41:12967-12974(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
    9. "Structure of the apo form of Bacillus stearothermophilus phosphofructokinase."
      Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.
      Biochemistry 51:769-775(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS).
    10. "Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase."
      Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.
      Biochemistry 52:5421-5429(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PHOSPHOENOLPYRUVIC ACID.

    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: October 1, 2014
    This is version 123 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.
    The phosphate group of phosphoenolpyruvate appears to bind in the same place as the beta-phosphate group of ADP.

    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

    External Data

    Dasty 3