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28  structures 4467  species 0  interactions 6166  sequences 16  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
EC number
CAS number 9031-46-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
phosphoribosyl pyrophosphate synthetase 1
Symbol PRPS1
Entrez 5631
HUGO 9462
OMIM 311850
RefSeq NM_002764
UniProt P60891
Other data
Locus Chr. X q21-q27
phosphoribosyl pyrophosphate synthetase 2
Symbol PRPS2
Entrez 5634
HUGO 9465
OMIM 311860
RefSeq NM_002765
UniProt P11908
Other data
Locus Chr. X pter-q21

Ribose-phosphate diphosphokinase (or phosphoribosyl pyrophosphate synthetase) is an enzyme that converts ribose 5-phosphate into phosphoribosyl pyrophosphate.

Its substrate is produced by the HMP Shunt Pathway from Glucose-6-Phosphate.

Its product acts as an essential component of the purine salvage pathway and the de novo synthesis of purines. Dysfunction of the enzyme would thereby undermine purine metabolism.

It is classified under EC

External links[edit]

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

External database links

This tab holds annotation information from the InterPro database.

No InterPro data for this Pfam family.

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 contains the following 6 members:

Pribosyl_synth Pribosyltran 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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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

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

Format an alignment

Representative proteomes NCBI

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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.

Representative proteomes NCBI
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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 HMMER3.

Pfam alignments:

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

This family is new in this Pfam release.

Seed source: pdb_2c4k; Jackhmmer:Q14558
Previous IDs: none
Type: Domain
Author: Coggill P
Number in seed: 11
Number in full: 6166
Average length of the domain: 127.90 aa
Average identity of full alignment: 40 %
Average coverage of the sequence by the domain: 39.16 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.2 27.0
Noise cut-off 26.9 26.9
Model length: 184
Family (HMM) version: 1
Download: download the raw HMM for this family

Species distribution

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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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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 28 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 seqence.

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