Summary
ADP-specific Phosphofructokinase/Glucokinase conserved region
In archaea a novel type of glycolytic pathway exists that is deviant from the classical Embden-Meyerhof pathway. This pathway utilises two novel proteins: an ADP-dependent Glucokinase and an ADP-dependent Phosphofructokinase. This conserved region is present at the C-terminal of both these proteins. Interestingly this family contains sequences from higher eukaryotes. [1,2,3].
Literature references
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Tuininga JE, Verhees CH, van der Oost J, Kengen SW, Stams AJ, de Vos WM; , J Biol Chem 1999;274:21023-21028.: Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus. PUBMED:10409652
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Verhees CH, Tuininga JE, Kengen SW, Stams AJ, van der Oost J, de Vos WM; , J Bacteriol 2001;183:7145-7153.: ADP-dependent phosphofructokinases in mesophilic and thermophilic methanogenic archaea. PUBMED:11717273
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Ronimus RS, de Heus E, Morgan HW; , Biochim Biophys Acta 2001;1517:384-391.: Sequencing, expression, characterisation and phylogeny of the ADP-dependent phosphofructokinase from the hyperthermophilic, euryarchaeal Thermococcus zilligii. PUBMED:11342216
InterPro entry IPR007666
Although ATP is the most common phosphoryl group donor for kinases, certain hyperthermophilic archaea, such as Thermococcus litoralis and Pyrococcus furiosus, utilise unusual ADP-dependent glucokinases (ADPGKs) and phosphofructokinases (ADPPKKs) in their glycolytic pathways PUBMED:11286887, PUBMED:12237466, PUBMED:12909015. ADPGKs and ADPPFKs exhibit significant similarity, and form an ADP-dependent kinase (ADPK) family, which was tentatively named the PFKC family PUBMED:11778837. A ~460-residue ADPK domain is also found in a bifunctional ADP-dependent gluco/phosphofructo- kinase (ADP-GK/PFK) from Methanocaldococcus jannaschii (Methanococcus jannaschii) as well as in homologous hypothetical proteins present in several eukaryotes PUBMED:11717273.
The whole structure of the ADPK domain can be divided into large and small alpha/beta subdomains. The larger subdomain, which carries the ADP binding site, consists of a twisted 12-stranded beta sheet flanked on both faces by 13 alpha helices and three 3(10) helices, forming an alpha/beta 3-layer sandwich. The smaller subdomain, which covers the active site, forms an alpha/beta two-layer structure containing 5 beta strands and four alpha helices. The ADP molecule is buried in a shallow pocket in the large subdomain. The binding of substrate sugar induces a structural change, the small domain closing to form a complete substrate sugar binding site PUBMED:11286887, PUBMED:12237466, PUBMED:12909015.
Clan
This family is a member of clan Ribokinase (CL0118), which contains the following 5 members:
ADP_PFK_GK Carb_kinase HK PfkB Phos_pyr_kinGene Ontology
| Molecular function | phosphotransferase activity, alcohol group as acceptor (GO:0016773) |
| Biological process | carbohydrate metabolic process (GO:0005975) |
External database links
| PANDIT: | PF04587 |
| SCOP: | 1l2l |
| SYSTERS: | ADP_PFK_GK |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_4731 (release 7.5) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Waterfield DI, Finn RD |
| Number in seed: | 9 |
| Number in full: | 96 |
| Average length of the domain: | 379.90 aa |
| Average identity of full alignment: | 26 % |
| Average coverage of the sequence by the domain: | 81.15 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 445 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ADP_PFK_GK domain has been found.
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