2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase catalyzes the pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin to form AMP and 6-hydroxymethyl-7,8-dihydropterin diphosphate
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) [Coenzyme transport ...
2-152
2.17e-63
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) [Coenzyme transport and metabolism]; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) is part of the Pathway/BioSystem: Folate biosynthesis
:
Pssm-ID: 440564 Cd Length: 155 Bit Score: 192.22 E-value: 2.17e-63
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) [Coenzyme transport ...
2-152
2.17e-63
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) [Coenzyme transport and metabolism]; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440564 Cd Length: 155 Bit Score: 192.22 E-value: 2.17e-63
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK). Folate derivatives are essential ...
2-126
1.30e-52
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK). Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is HPPK which catalyzes pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The functional enzyme is a monomer. Mammals lack many of the enzymes in the folate pathway including, HPPK.
Pssm-ID: 238269 Cd Length: 128 Bit Score: 163.80 E-value: 1.30e-52
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; This model describes the ...
2-130
1.38e-39
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; This model describes the folate biosynthesis enzyme 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. Alternate names include 6-hydroxymethyl-7,8-dihydropterin diphosphokinase and 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (HPPK). The extreme C-terminal region, of typically eight to thirty residues, is not included in the model. This enzyme may be found as a fusion protein with other enzymes of folate biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273658 Cd Length: 129 Bit Score: 130.86 E-value: 1.38e-39
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) [Coenzyme transport ...
2-152
2.17e-63
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) [Coenzyme transport and metabolism]; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440564 Cd Length: 155 Bit Score: 192.22 E-value: 2.17e-63
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK). Folate derivatives are essential ...
2-126
1.30e-52
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK). Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is HPPK which catalyzes pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The functional enzyme is a monomer. Mammals lack many of the enzymes in the folate pathway including, HPPK.
Pssm-ID: 238269 Cd Length: 128 Bit Score: 163.80 E-value: 1.30e-52
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; This model describes the ...
2-130
1.38e-39
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; This model describes the folate biosynthesis enzyme 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. Alternate names include 6-hydroxymethyl-7,8-dihydropterin diphosphokinase and 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (HPPK). The extreme C-terminal region, of typically eight to thirty residues, is not included in the model. This enzyme may be found as a fusion protein with other enzymes of folate biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273658 Cd Length: 129 Bit Score: 130.86 E-value: 1.38e-39
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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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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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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Domains are color coded according to superfamilies
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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,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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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