Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ...
1-201
1.39e-113
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to PFK family that includes ATP- and pyrophosphate (PPi)- dependent phosphofructokinases. Some members evolved by gene duplication and thus have a large C-terminal/N-terminal extension comprising a second PFK domain. Generally, ATP-PFKs are allosteric homotetramers, and PPi-PFKs are dimeric and nonallosteric except for plant PPi-PFKs which are allosteric heterotetramers.
The actual alignment was detected with superfamily member cd00764:
Pssm-ID: 469655 [Multi-domain] Cd Length: 762 Bit Score: 340.65 E-value: 1.39e-113
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ...
1-201
1.39e-113
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 340.65 E-value: 1.39e-113
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ...
1-184
1.29e-90
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 280.76 E-value: 1.29e-90
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ...
1-201
1.39e-113
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 340.65 E-value: 1.39e-113
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ...
1-184
1.29e-90
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 280.76 E-value: 1.29e-90
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ...
1-153
3.15e-11
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to PFK family that includes ATP- and pyrophosphate (PPi)- dependent phosphofructokinases. Some members evolved by gene duplication and thus have a large C-terminal/N-terminal extension comprising a second PFK domain. Generally, ATP-PFKs are allosteric homotetramers, and PPi-PFKs are dimeric and nonallosteric except for plant PPi-PFKs which are allosteric heterotetramers.
Pssm-ID: 238216 [Multi-domain] Cd Length: 338 Bit Score: 61.16 E-value: 3.15e-11
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ...
1-172
9.15e-11
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include bacterial ATP-dependent phosphofructokinases. These are allosrterically regulated homotetramers; the subunits are of about 320 amino acids.
Pssm-ID: 238388 [Multi-domain] Cd Length: 317 Bit Score: 59.73 E-value: 9.15e-11
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ...
1-199
1.35e-10
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 59.84 E-value: 1.35e-10
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ...
1-157
1.50e-07
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 50.80 E-value: 1.50e-07
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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of your query sequence and the protein sequences used to curate the domain model,
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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