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647  structures 8999  species 0  interactions 55659  sequences 216  architectures

Family: Pribosyltran (PF00156)

Summary: Phosphoribosyl transferase domain

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

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

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 transferase domain Provide feedback

This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7, P07672. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase P51900. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8 P36766. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1 P09329. Amidophosphoribosyltransferase EC:2.4.2.14 P00496. Orotate phosphoribosyl-transferase EC:2.4.2.10 P11172. Uracil phosphoribosyl-transferase EC:2.4.2.9 P25532. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22 P00501. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain [1].

Literature references

  1. Islam MR, Kim H, Kang SW, Kim JS, Jeong YM, Hwang HJ, Lee SY, Woo JC, Kim SG;, Plant Mol Biol. 2007;63:465-477.: Functional characterization of a gene encoding a dual domain for uridine kinase and uracil phosphoribosyltransferase in Arabidopsis thaliana. PUBMED:17143579 EPMC:17143579


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000836

This entry refers to the phosphoribosyl transferase (PRT) type I domain. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrpphosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. This domain is found in a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC , hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC , ribose-phosphate pyrophosphokinase EC , amidophosphoribosyltransferase EC , orotate phosphoribosyltransferase EC , uracil phosphoribosyltransferase EC , and xanthine-guanine phosphoribosyltransferase EC . In Arabidopsis, at the very N terminus of this domain is the P-Loop NTPase domain [ PUBMED:17143579 , PUBMED:11751055 , PUBMED:18550080 , PUBMED:15689504 , PUBMED:18399692 , PUBMED:12808089 , PUBMED:8894695 , PUBMED:22075667 , PUBMED:15096496 , PUBMED:7030616 , PUBMED:6105839 , PUBMED:21366534 , PUBMED:18535147 ].

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

Alignments

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
(26)
Full
(55659)
Representative proteomes UniProt
(246480)
RP15
(7754)
RP35
(27059)
RP55
(55978)
RP75
(94783)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

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

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

Format an alignment

  Seed
(26)
Full
(55659)
Representative proteomes UniProt
(246480)
RP15
(7754)
RP35
(27059)
RP55
(55978)
RP75
(94783)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

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.

  Seed
(26)
Full
(55659)
Representative proteomes UniProt
(246480)
RP15
(7754)
RP35
(27059)
RP55
(55978)
RP75
(94783)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download    

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 View help on the curation process

Seed source: Bateman A
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Sonnhammer ELL , Finn RD , Eberhardt R
Number in seed: 26
Number in full: 55659
Average length of the domain: 142.1 aa
Average identity of full alignment: 16 %
Average coverage of the sequence by the domain: 56.34 %

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 26.3 26.3
Trusted cut-off 26.3 26.3
Noise cut-off 26.2 26.2
Model length: 158
Family (HMM) version: 30
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

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 Pribosyltran domain has been found. There are 647 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
A0A044RFA9 View 3D Structure Click here
A0A044U814 View 3D Structure Click here
A0A044UNW2 View 3D Structure Click here
A0A077Z6Y8 View 3D Structure Click here
A0A077ZBM1 View 3D Structure Click here
A0A077ZKG1 View 3D Structure Click here
A0A0D2EU99 View 3D Structure Click here
A0A0D2G625 View 3D Structure Click here
A0A0D2H8S9 View 3D Structure Click here
A0A0D2HCB5 View 3D Structure Click here
A0A0H3GJG3 View 3D Structure Click here
A0A0H3GSB1 View 3D Structure Click here
A0A0H3GSW8 View 3D Structure Click here
A0A0H3GXD7 View 3D Structure Click here
A0A0H3H133 View 3D Structure Click here
A0A0J9Y162 View 3D Structure Click here
A0A0K0E837 View 3D Structure Click here
A0A0K0EEU6 View 3D Structure Click here
A0A0K0EML5 View 3D Structure Click here
A0A0K0EML6 View 3D Structure Click here
A0A0K0IZE9 View 3D Structure Click here
A0A0N4U2G8 View 3D Structure Click here
A0A0N4U623 View 3D Structure Click here
A0A0N4UMW6 View 3D Structure Click here
A0A0P0WCD3 View 3D Structure Click here
A0A0P0WIZ3 View 3D Structure Click here
A0A0R0HLC7 View 3D Structure Click here
A0A0R4J336 View 3D Structure Click here
A0A0R4J3H2 View 3D Structure Click here
A0A0R4J587 View 3D Structure Click here
A0A158Q4K2 View 3D Structure Click here
A0A175VQH6 View 3D Structure Click here
A0A175W272 View 3D Structure Click here
A0A175W769 View 3D Structure Click here
A0A183XV84 View 3D Structure Click here
A0A1C1CPV8 View 3D Structure Click here
A0A1C1CR36 View 3D Structure Click here
A0A1C1CWC8 View 3D Structure Click here
A0A1C1CZT9 View 3D Structure Click here
A0A1D6E6M0 View 3D Structure Click here