Summary: Phosphoribosyl synthetase-associated domain
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This is the Wikipedia entry entitled "Ribose-phosphate diphosphokinase". More...
Ribose-phosphate diphosphokinase Edit Wikipedia article
Ribose-phosphate diphosphokinase (or phosphoribosyl pyrophosphate synthetase) is an enzyme which converts ribose 5-phosphate into phosphoribosyl pyrophosphate.
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Phosphoribosyl synthetase-associated domain Provide feedback
This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.
Literature references
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Katashima R, Iwahana H, Fujimura M, Yamaoka T, Ishizuka T, Tatibana M, Itakura M;, Biochim Biophys Acta. 1998;1396:245-250.: Molecular cloning of a human cDNA for the 41-kDa phosphoribosylpyrophosphate synthetase-associated protein. PUBMED:9545573 EPMC:9545573
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Iizasa T;, Nihon Rinsho. 2008;66:694-698.: [Increased activity of PRPP synthetase]. PUBMED:18409517 EPMC:18409517
Internal database links
SCOOP: | NIT Pribosyltran PRTase_2 UPRTase |
Similarity to PfamA using HHSearch: | Pribosyltran |
This tab holds annotation information from the InterPro database.
InterPro entry IPR005946
Ribose-phosphate diphosphokinase, also known as ribose-phosphate pyrophosphokinase (RPPK), or phosphoribosyldiphosphate synthetase ( EC ), catalyses the transfer of an intact diphosphate (PP) group from ATP to ribose-5-phosphate (R-5-P), which results in the formation of AMP and 5-phospho-D-ribosyl--1-diphosphate (PRPP).
PRPP is an essential precursor for purine and pyrimidine nucleotides, both in the de novo synthesis and in the salvage pathway, as well as in the synthesis of pyridine nucleotide coenzymes. The activity of PPPK is highly regulated. Besides competitive inhibition at the substrate binding sites, most RPPKs are regulated in an allosteric manner, in which ADP generally acts as the most potent inhibitor. In some systems, close homologues lacking enzymatic activity exist and perform regulatory functions.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | magnesium ion binding (GO:0000287) |
ribose phosphate diphosphokinase activity (GO:0004749) | |
Biological process | nucleotide biosynthetic process (GO:0009165) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan PRTase-like (CL0533), which has the following description:
This superfamily of phosphoribosyl-transferases (PRTases) and phosphoribosyl-pyrophosphate synthetase-like protein families is characterised by a core fold of three layers, a/b/a with a mixed beta-sheet of six strands. In one of the families consists of two domains of this fold.
The clan contains the following 7 members:
Pribosyl_synth Pribosyltran Pribosyltran_N PRTase_1 PRTase_2 PRTase_3 UPRTaseAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (6) |
Full (14886) |
Representative proteomes | UniProt (50491) |
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RP15 (2225) |
RP35 (6747) |
RP55 (13638) |
RP75 (21879) |
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Jalview | |||||||
HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (6) |
Full (14886) |
Representative proteomes | UniProt (50491) |
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RP15 (2225) |
RP35 (6747) |
RP55 (13638) |
RP75 (21879) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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's seed alignment. 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 alignment.
Note: You can also download the data file for the tree.
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: | pdb_2c4k; Jackhmmer:Q14558 |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Coggill P |
Number in seed: | 6 |
Number in full: | 14886 |
Average length of the domain: | 128.9 aa |
Average identity of full alignment: | 37 % |
Average coverage of the sequence by the domain: | 38.13 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 184 | ||||||||||||
Family (HMM) version: | 9 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Selections
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. 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 PDBe 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 Pribosyl_synth domain has been found. There are 54 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.