ATP-dependent 6-phosphofructokinase
Details
- Name
- ATP-dependent 6-phosphofructokinase
- Synonyms
- 2.7.1.11
- ATP-PFK
- pfk
- Phosphohexokinase
- Gene Name
- pfkA
- Organism
- Geobacillus stearothermophilus
- Amino acid sequence
>lcl|BSEQ0019188|ATP-dependent 6-phosphofructokinase MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDI IHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCV GVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWS GLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGF ETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL ANKHTIDQRMYALSKELSI
- Number of residues
- 319
- Molecular Weight
- 34118.62
- Theoretical pI
- 6.96
- GO Classification
- Functions6-phosphofructokinase activity / ATP binding / metal ion bindingProcessesfructose 6-phosphate metabolic processComponentscytoplasm
- General Function
- Metal ion binding
- Specific Function
- Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
- Pfam Domain Function
- PFK (PF00365)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0003601|960 bp GTGAAACGCATTGGTGTGTTGACAAGCGGCGGCGACTCGCCGGGAATGAATGCGGCCATT CGCTCGGTTGTCCGCAAAGCGATTTACCACGGTGTGGAAGTGTACGGCGTTTATCACGGG TATGCCGGACTGATCGCCGGCAACATTAAAAAGCTGGAAGTCGGCGATGTCGGGGATATT ATCCACCGTGGCGGCACGATACTCTATACGGCCCGCTGTCCGGAATTTAAGACGGAAGAA GGTCAGAAAAAAGGGATCGAGCAGCTGAAAAAGCACGGCATTGAAGGGCTGGTCGTCATC GGCGGCGACGGTTCGTACCAAGGGGCGAAAAAACTGACCGAGCACGGCTTTCCGTGCGTC GGCGTGCCGGGGACGATTGACAACGACATTCCGGGCACTGATTTTACGATCGGGTTTGAC ACGGCGCTCAATACGGTCATTGATGCCATCGACAAAATCCGCGACACGGCGACGTCGCAC GAGCGGACGTACGTCATCGAAGTGATGGGCCGCCATGCCGGCGACATCGCCTTATGGTCG GGGCTGGCCGGCGGGGCGGAAACGATTTTAATTCCGGAAGCCGATTATGATATGAACGAC GTCATCGCCCGCTTAAAGCGCGGCCATGAGCGCGGCAAAAAACATAGCATCATCATCGTG GCGGAAGGAGTTGGAAGCGGCGTCGACTTCGGCCGGCAAATCCAGGAAGCGACCGGCTTT GAGACGCGTGTGACGGTGCTTGGCCACGTGCAGCGCGGCGGGTCGCCCACGGCGTTTGAC CGCGTGCTCGCGAGCCGCCTCGGCGCCCGGGCGGTCGAGCTGTTGCTCGAAGGAAAAGGC GGGCGCTGCGTCGGCATCCAAAACAACCAGCTCGTCGACCATGACATCGCGGAGGCGCTA GCCAACAAACATACGATTGATCAGCGGATGTACGCATTGTCGAAAGAATTGTCCATTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00512 UniProtKB Entry Name PFKA_GEOSE GenBank Protein ID 143312 GenBank Gene ID M15643 - General References
- French BA, Chang SH: Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene. Gene. 1987;54(1):65-71. [Article]
- Kolb E, Hudson PJ, Harris JI: Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus. Eur J Biochem. 1980 Jul;108(2):587-97. [Article]
- Sakai H, Ohta T: 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. Eur J Biochem. 1993 Feb 1;211(3):851-9. [Article]
- Byrnes M, Zhu X, Younathan ES, Chang SH: Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme. Biochemistry. 1994 Mar 22;33(11):3424-31. [Article]
- Evans PR, Hudson PJ: Structure and control of phosphofructokinase from Bacillus stearothermophilus. Nature. 1979 Jun 7;279(5713):500-4. [Article]
- Evans PR, Farrants GW, Hudson PJ: Phosphofructokinase: structure and control. Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):53-62. [Article]
- Schirmer T, Evans PR: Structural basis of the allosteric behaviour of phosphofructokinase. Nature. 1990 Jan 11;343(6254):140-5. [Article]
- Riley-Lovingshimer MR, Ronning DR, Sacchettini JC, Reinhart GD: Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus. Biochemistry. 2002 Oct 29;41(43):12967-74. [Article]
- Mosser R, Reddy MC, Bruning JB, Sacchettini JC, Reinhart GD: Structure of the apo form of Bacillus stearothermophilus phosphofructokinase. Biochemistry. 2012 Jan 24;51(3):769-75. doi: 10.1021/bi201548p. Epub 2012 Jan 11. [Article]
- Mosser R, Reddy MC, Bruning JB, Sacchettini JC, Reinhart GD: Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase. Biochemistry. 2013 Aug 13;52(32):5421-9. doi: 10.1021/bi4002503. Epub 2013 Jul 31. [Article]