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Phosphofructokinase superfamily
SCOP classification
Superfamily statistics
Functional annotation
| General category | Metabolism |
| Detailed category | Energy |
Function annotation of SCOP domain superfamilies
InterPro annotation
| Cross references | IPR000023 SSF53784 Protein matches |
| Abstract | The enzyme-catalysed transfer of a phosphoryl group from ATP is an
important reaction in a wide variety of biological processes [ 2953977]. One
enzyme that utilises this reaction is phosphofructokinase (PFK), which
catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-
bisphosphate, a key regulatory step in the glycolytic pathway [12023862, 7825568].
PFK exists as a homotetramer in bacteria and mammals (where each monomer
possesses 2 similar domains), and as an octomer in yeast (where there are
4 alpha- (PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian
monomers, possessing 2 similar domains [7825568]). PFK is ~300 amino acids in length, and structural studies of the
bacterial enzyme have shown it comprises two similar (alpha/beta) lobes: one involved in
ATP binding and the other housing both the substrate-binding site and the allosteric site (a regulatory binding site distinct from the active site, but that affects enzyme
activity). The identical tetramer subunits adopt 2
different conformations: in a 'closed' state, the bound magnesium ion
bridges the phosphoryl groups of the enzyme products (ADP and fructose-1,6-
bisphosphate); and in an 'open' state, the magnesium ion binds only the ADP
[2975709], as the 2 products are now further apart. These conformations are
thought to be successive stages of a reaction pathway that requires subunit
closure to bring the 2 molecules sufficiently close to react [2975709].
Deficiency in PFK leads to glycogenosis type VII (Tauri's disease), an
autosomal recessive disorder characterised by severe nausea, vomiting,
muscle cramps and myoglobinuria in response to bursts of intense or
vigorous exercise [7825568]. Sufferers are usually able to lead a reasonably
ordinary life by learning to adjust activity levels [7825568]. |
InterPro database
PDBeMotif information about ligands, sequence and structure motifs
PDBeMotif resource
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation ]
Internal database links
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Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.
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Alignments of sequences to 3 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.
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Browse and view proteins in genomes which have
different domain combinations including a Phosphofructokinase domain.
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Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
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Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.
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There are 3 hidden Markov models representing the Phosphofructokinase superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.
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Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Internal database links ]
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