2.7.1.146: ADP-specific phosphofructokinase
This is an abbreviated version!
For detailed information about ADP-specific phosphofructokinase, go to the full flat file.
Word Map on EC 2.7.1.146
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2.7.1.146
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hyperthermophilic
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embden-meyerhof
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archaeon
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methanococcus
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jannaschii
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amp
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furiosus
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thermococcus
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atp-pfks
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phosphofructokinases
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ppi-dependent
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fructose-1,6-bisphosphate
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sulfate-reducing
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archaeoglobus
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fulgidus
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pyrophosphate-dependent
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zilligii
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thermococcales
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eucarya
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horikoshii
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adp-forming
- 2.7.1.146
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hyperthermophilic
-
embden-meyerhof
- archaeon
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methanococcus
- jannaschii
- amp
- furiosus
- thermococcus
- atp-pfks
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phosphofructokinases
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ppi-dependent
- fructose-1,6-bisphosphate
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sulfate-reducing
-
archaeoglobus
- fulgidus
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pyrophosphate-dependent
- zilligii
- thermococcales
- eucarya
- horikoshii
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adp-forming
Reaction
Synonyms
ADP dependent phosphofructokinase, ADP-6-phosphofructokinase, ADP-dependent 6-phosphofructokinase, ADP-dependent glucokinase, ADP-dependent glucokinase/phosphofructokinase, ADP-dependent PFK, ADP-dependent phosphofructokinase, ADP-GK, ADP-Pfk, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, MevePFK/GK, MJ1604, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, PFK, PFK-ADP, pfkC, PhPFK, TK0376, TLPFK
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General Information
General Information on EC 2.7.1.146 - ADP-specific phosphofructokinase
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evolution
physiological function
additional information
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consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
evolution
kinetic analyses of the phosphofructokinase annotated enzyme from Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
evolution
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Analsis of enzyme ADP-PFK structure (PDB ID 1U2X) from Pyrococcus furiosus. Sequences and structures comparisons. Pyrococcus horikoshii posseses a phosphofructokinase and a glucokinase
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons
evolution
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
evolution
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei possesses a bifunctional MmazPFK/GK
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei possesses a bifunctional MmazPFK/GK
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evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei possesses a bifunctional MmazPFK/GK
-
evolution
-
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei possesses a bifunctional MmazPFK/GK
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei possesses a bifunctional MmazPFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Analsis of enzyme ADP-PFK structure (PDB ID 1U2X) from Pyrococcus furiosus. Sequences and structures comparisons. Pyrococcus horikoshii posseses a phosphofructokinase and a glucokinase
-
evolution
-
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei possesses a bifunctional MmazPFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
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the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
key enzyme of the modified Embden-Meyerhof pathway of heterotrophic and chemolithoautotrophic archaea
physiological function
the phosphofructokinase activity of the enzyme is not allosterically regulated
physiological function
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the phosphofructokinase activity of the enzyme is not allosterically regulated
-
physiological function
-
key enzyme of the modified Embden-Meyerhof pathway of heterotrophic and chemolithoautotrophic archaea
-
physiological function
-
the phosphofructokinase activity of the enzyme is not allosterically regulated
-
enzyme structure and homology modeling
additional information
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-