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54  structures 8088  species 0  interactions 14886  sequences 87  architectures

Family: Pribosyl_synth (PF14572)

Summary: Phosphoribosyl synthetase-associated domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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.

It is classified under EC

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:, phosphoribosyl-pyrophosphate transferase.

Literature references

  1. 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

  2. Iizasa T;, Nihon Rinsho. 2008;66:694-698.: [Increased activity of PRPP synthetase]. PUBMED:18409517 EPMC:18409517

Internal database links

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.

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 UPRTase


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.

Representative proteomes UniProt
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

Representative proteomes UniProt

Download options

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.

Representative proteomes UniProt
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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...


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 View help on the curation process

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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 27.0
Noise cut-off 26.9 26.9
Model length: 184
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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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The tree shows the occurrence of this domain across different species. More...


Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.


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.

Protein Predicted structure External Information
A0A044TSD7 View 3D Structure Click here
A0A044VB87 View 3D Structure Click here
A0A077Z3R4 View 3D Structure Click here
A0A077ZNC3 View 3D Structure Click here
A0A0D2GQ57 View 3D Structure Click here
A0A0D2GSR9 View 3D Structure Click here
A0A0D2GSV1 View 3D Structure Click here
A0A0D2H2M8 View 3D Structure Click here
A0A0G2JSV3 View 3D Structure Click here
A0A0G2KZE8 View 3D Structure Click here
A0A0H3GPQ6 View 3D Structure Click here
A0A0H5SQT7 View 3D Structure Click here
A0A0K0DX06 View 3D Structure Click here
A0A0K0E2G6 View 3D Structure Click here
A0A0K0EDZ6 View 3D Structure Click here
A0A0N4U9U5 View 3D Structure Click here
A0A0N4UA03 View 3D Structure Click here
A0A175VX90 View 3D Structure Click here
A0A175W1H8 View 3D Structure Click here
A0A175WBD9 View 3D Structure Click here
A0A1C1CCF3 View 3D Structure Click here
A0A1C1CEY0 View 3D Structure Click here
A0A1C1CXV7 View 3D Structure Click here
A0A2K6VPT9 View 3D Structure Click here
A0A3P7DHZ6 View 3D Structure Click here
A0A3P7DX94 View 3D Structure Click here
A0A5S6PFN2 View 3D Structure Click here
A2VDS0 View 3D Structure Click here
A3AD51 View 3D Structure Click here
A4HTJ9 View 3D Structure Click here
A4HTP6 View 3D Structure Click here
A4I955 View 3D Structure Click here
A4IDV3 View 3D Structure Click here
B4FQE0 View 3D Structure Click here
B7IFM5 View 3D Structure Click here
B7ZZ73 View 3D Structure Click here
B8GZV1 View 3D Structure Click here
C0NDH6 View 3D Structure Click here
C0NJY6 View 3D Structure Click here
C0NKX2 View 3D Structure Click here